Source 1primary paper2013Biochemistry
Toolkit/PpSB1-LOV
PpSB1-LOV
Also known as: slow cycling bacterial short LOV photoreceptor PpSB1-LOV
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
PpSB1-LOV is a bacterial short LOV photosensory domain from Pseudomonas putida KT2440 with a light-induced flavin-cysteinyl photo-adduct and exceptionally slow dark recovery. It has been characterized as a compact LOV building block whose photocycle kinetics can be tuned by conserved hydrophobic-pocket mutation, including the I48T variant that accelerates adduct rupture while remaining structurally and mechanistically benign.
Usefulness & Problems
Why this is useful
PpSB1-LOV is useful as a compact LOV module with a well-characterized long-lived signaling state, which is relevant for designing genetically encoded photoswitches and other LOV-based optogenetic tools. The literature specifically supports its value for tuning dark-recovery behavior and thereby adjusting sensor on/off kinetics and steady-state on/off equilibria.
Source:
PpSB1-LOV is a named short LOV protein discussed as part of a pair with markedly different dark recovery kinetics. The paper treats such proteins as candidate building blocks for genetically encoded photoswitches.
Source:
LOV-based optogenetic tool design
Source:
providing a slow- or fast-recovery LOV building block
Problem solved
This domain helps address the problem of obtaining LOV photosensory modules with defined and engineerable dark-recovery times. The cited work shows that conserved-pocket mutations can modulate photo-adduct lifetime in PpSB1-LOV and related LOV proteins, providing a route to tune signaling-state duration.
Source:
It provides a compact LOV photosensory module with characterized recovery behavior that may be useful in photoswitch design. The family architecture is presented as prototypic for more complex LOV systems.
Source:
offers a short LOV photoreceptor building block with characterized dark recovery behavior
Published Workflows
Objective: Characterize distribution, phylogeny, photochemical properties, and structural features of short LOV proteins to assess their suitability as building blocks for LOV-based optogenetic tools.
Why it works: The workflow combines comparative family analysis with photochemical and structural characterization to identify conserved kinetic and architectural features that may generalize to tool design. The authors argue that the prototypic architecture of short LOV proteins, conserved in more complex LOV photoreceptors, makes them informative building blocks for genetically encoded photoswitches.
variation in adduct-state lifetimeterminal-extension-dependent folding and structural integrityhelical C-terminal extensionscoiled-coil formation in dimeric full-length proteinsdistribution and phylogeny analysistruncation studiescircular dichroismsolution nuclear magnetic resonancebioinformatic analysis
Stages
- 1.Distribution and phylogeny analysis of short LOV proteins(in_silico_filter)
The authors first examined distribution and phylogeny to understand family prevalence and conservation before deeper photochemical and structural characterization.
Selection: distribution and phylogeny of the short LOV protein family
- 2.Photochemical characterization of fast- and slow-reverting short LOV proteins(functional_characterization)
Photochemical characterization establishes the range of adduct-state lifetimes that may be useful for engineering photoswitch behavior.
Selection: dark recovery kinetic behavior including fast- and slow-reverting proteins
- 3.Truncation-based structural integrity and folding assessment(secondary_characterization)
This stage tests whether terminal regions outside the LOV core are required to maintain the protein architecture needed for use as engineering building blocks.
Selection: effect of removing N- and C-terminal extensions on protein integrity and folding
- 4.Structural verification of C-terminal extension helices in solution(confirmatory_validation)
Circular dichroism and solution NMR were used to verify the structural interpretation of the C-terminal extensions in solution.
Selection: verification of independently folding helical structures in the short C-terminal extensions
- 5.Bioinformatic inference of coiled coils in full-length dimers(secondary_characterization)
Bioinformatic analysis extends the solution-state structural observations to a proposed arrangement in the dimeric full-length proteins.
Selection: predicted coiled-coil formation of structural elements in dimeric full-length proteins
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
dark-state adduct ruptureHeterodimerizationlight-induced flavin-cysteinyl photo-adduct formationlight-induced flavin-cysteinyl photo-adduct formation and dark-state adduct rupturephotocycle dark-recovery tuning by conserved hydrophobic-pocket mutationphotocycle dark-recovery tuning via conserved hydrophobic-pocket mutationTarget processes
No target processes tagged yet.
Input: Light
Implementation Constraints
PpSB1-LOV is a short LOV protein from Pseudomonas putida KT2440 and operates through the canonical LOV flavin-cysteinyl photo-adduct cycle, so flavin binding is implicit in its function. The extracted evidence indicates that intact N- and C-terminal extensions appear important for proper folding and structural integrity, and the I48T mutation in a conserved hydrophobic pocket is a documented strategy to accelerate dark recovery.
The supplied evidence does not show that PpSB1-LOV alone functions as a complete optogenetic actuator in a target cellular system. Available claims focus on photocycle characterization and mutational tuning, with limited direct validation of downstream biological control or application-specific performance.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2primary paper2022Photochemical & Photobiological Sciences
Source 3primary paper2021FEBS Journal
Ranked Claims
The identified conserved-pocket mutations should find application in dark-recovery tuning of optogenetic tools and LOV photoreceptors.
Given the conserved nature of the corresponding structural region, the here identified mutations should find application in dark-recovery tuning of optogenetic tools and LOV photoreceptors, alike.
The identified conserved-pocket mutations should find application in dark-recovery tuning of optogenetic tools and LOV photoreceptors.
Given the conserved nature of the corresponding structural region, the here identified mutations should find application in dark-recovery tuning of optogenetic tools and LOV photoreceptors, alike.
The identified conserved-pocket mutations should find application in dark-recovery tuning of optogenetic tools and LOV photoreceptors.
Given the conserved nature of the corresponding structural region, the here identified mutations should find application in dark-recovery tuning of optogenetic tools and LOV photoreceptors, alike.
The identified conserved-pocket mutations should find application in dark-recovery tuning of optogenetic tools and LOV photoreceptors.
Given the conserved nature of the corresponding structural region, the here identified mutations should find application in dark-recovery tuning of optogenetic tools and LOV photoreceptors, alike.
The identified conserved-pocket mutations should find application in dark-recovery tuning of optogenetic tools and LOV photoreceptors.
Given the conserved nature of the corresponding structural region, the here identified mutations should find application in dark-recovery tuning of optogenetic tools and LOV photoreceptors, alike.
The identified conserved-pocket mutations should find application in dark-recovery tuning of optogenetic tools and LOV photoreceptors.
Given the conserved nature of the corresponding structural region, the here identified mutations should find application in dark-recovery tuning of optogenetic tools and LOV photoreceptors, alike.
The identified conserved-pocket mutations should find application in dark-recovery tuning of optogenetic tools and LOV photoreceptors.
Given the conserved nature of the corresponding structural region, the here identified mutations should find application in dark-recovery tuning of optogenetic tools and LOV photoreceptors, alike.
Additional pocket mutations in PpSB1-LOV and homologous mutations in YtvA and the Avena sativa LOV2 domain produce similarly altered kinetics.
Additional mutations within the pocket of PpSB1-LOV and the introduction of homologous mutations in the LOV photoreceptor YtvA of Bacillus subtilis and the Avena sativa LOV2 domain result in similarly altered kinetics.
Additional pocket mutations in PpSB1-LOV and homologous mutations in YtvA and the Avena sativa LOV2 domain produce similarly altered kinetics.
Additional mutations within the pocket of PpSB1-LOV and the introduction of homologous mutations in the LOV photoreceptor YtvA of Bacillus subtilis and the Avena sativa LOV2 domain result in similarly altered kinetics.
Additional pocket mutations in PpSB1-LOV and homologous mutations in YtvA and the Avena sativa LOV2 domain produce similarly altered kinetics.
Additional mutations within the pocket of PpSB1-LOV and the introduction of homologous mutations in the LOV photoreceptor YtvA of Bacillus subtilis and the Avena sativa LOV2 domain result in similarly altered kinetics.
Additional pocket mutations in PpSB1-LOV and homologous mutations in YtvA and the Avena sativa LOV2 domain produce similarly altered kinetics.
Additional mutations within the pocket of PpSB1-LOV and the introduction of homologous mutations in the LOV photoreceptor YtvA of Bacillus subtilis and the Avena sativa LOV2 domain result in similarly altered kinetics.
Additional pocket mutations in PpSB1-LOV and homologous mutations in YtvA and the Avena sativa LOV2 domain produce similarly altered kinetics.
Additional mutations within the pocket of PpSB1-LOV and the introduction of homologous mutations in the LOV photoreceptor YtvA of Bacillus subtilis and the Avena sativa LOV2 domain result in similarly altered kinetics.
Additional pocket mutations in PpSB1-LOV and homologous mutations in YtvA and the Avena sativa LOV2 domain produce similarly altered kinetics.
Additional mutations within the pocket of PpSB1-LOV and the introduction of homologous mutations in the LOV photoreceptor YtvA of Bacillus subtilis and the Avena sativa LOV2 domain result in similarly altered kinetics.
Additional pocket mutations in PpSB1-LOV and homologous mutations in YtvA and the Avena sativa LOV2 domain produce similarly altered kinetics.
Additional mutations within the pocket of PpSB1-LOV and the introduction of homologous mutations in the LOV photoreceptor YtvA of Bacillus subtilis and the Avena sativa LOV2 domain result in similarly altered kinetics.
Mutations that alter the lifetime of the photo-adduct signaling state can tune LOV sensor on/off kinetics and steady-state on/off equilibria.
Mutations that alter the lifetime of the photo-adduct signaling state represent a convenient handle to tune LOV sensor on/off kinetics and, thus, steady-state on/off equilibria of the photoreceptor (or optogenetic switch).
LOV photoreceptors have been broadly used as sensor domains for the construction of optogenetic tools.
LOV photoreceptors are widely distributed throughout all kingdoms of life, and have in recent years, due to their modular nature, been broadly used as sensor domains for the construction of optogenetic tools.
In PpSB1-LOV, the I48T mutation accelerates adduct rupture and is structurally and mechanistically benign, with unaltered light-induced structural changes by NMR spectroscopy and X-ray crystallography.
Using the slow cycling bacterial short LOV photoreceptor PpSB1-LOV, we show that the I48T mutation within this pocket, which accelerates adduct rupture, is otherwise structurally and mechanistically benign, i.e., light-induced structural changes, as probed by NMR spectroscopy and X-ray crystallography, are not altered in the variant.
In PpSB1-LOV, the I48T mutation accelerates adduct rupture and is structurally and mechanistically benign, with unaltered light-induced structural changes by NMR spectroscopy and X-ray crystallography.
Using the slow cycling bacterial short LOV photoreceptor PpSB1-LOV, we show that the I48T mutation within this pocket, which accelerates adduct rupture, is otherwise structurally and mechanistically benign, i.e., light-induced structural changes, as probed by NMR spectroscopy and X-ray crystallography, are not altered in the variant.
In PpSB1-LOV, the I48T mutation accelerates adduct rupture and is structurally and mechanistically benign, with unaltered light-induced structural changes by NMR spectroscopy and X-ray crystallography.
Using the slow cycling bacterial short LOV photoreceptor PpSB1-LOV, we show that the I48T mutation within this pocket, which accelerates adduct rupture, is otherwise structurally and mechanistically benign, i.e., light-induced structural changes, as probed by NMR spectroscopy and X-ray crystallography, are not altered in the variant.
In PpSB1-LOV, the I48T mutation accelerates adduct rupture and is structurally and mechanistically benign, with unaltered light-induced structural changes by NMR spectroscopy and X-ray crystallography.
Using the slow cycling bacterial short LOV photoreceptor PpSB1-LOV, we show that the I48T mutation within this pocket, which accelerates adduct rupture, is otherwise structurally and mechanistically benign, i.e., light-induced structural changes, as probed by NMR spectroscopy and X-ray crystallography, are not altered in the variant.
In PpSB1-LOV, the I48T mutation accelerates adduct rupture and is structurally and mechanistically benign, with unaltered light-induced structural changes by NMR spectroscopy and X-ray crystallography.
Using the slow cycling bacterial short LOV photoreceptor PpSB1-LOV, we show that the I48T mutation within this pocket, which accelerates adduct rupture, is otherwise structurally and mechanistically benign, i.e., light-induced structural changes, as probed by NMR spectroscopy and X-ray crystallography, are not altered in the variant.
In PpSB1-LOV, the I48T mutation accelerates adduct rupture and is structurally and mechanistically benign, with unaltered light-induced structural changes by NMR spectroscopy and X-ray crystallography.
Using the slow cycling bacterial short LOV photoreceptor PpSB1-LOV, we show that the I48T mutation within this pocket, which accelerates adduct rupture, is otherwise structurally and mechanistically benign, i.e., light-induced structural changes, as probed by NMR spectroscopy and X-ray crystallography, are not altered in the variant.
In PpSB1-LOV, the I48T mutation accelerates adduct rupture and is structurally and mechanistically benign, with unaltered light-induced structural changes by NMR spectroscopy and X-ray crystallography.
Using the slow cycling bacterial short LOV photoreceptor PpSB1-LOV, we show that the I48T mutation within this pocket, which accelerates adduct rupture, is otherwise structurally and mechanistically benign, i.e., light-induced structural changes, as probed by NMR spectroscopy and X-ray crystallography, are not altered in the variant.
A conserved hydrophobic pocket has mutations with strong impact on adduct-state lifetime across different LOV photoreceptor families.
we identify a conserved hydrophobic pocket for which mutations have a strong impact on the adduct-state lifetime across different LOV photoreceptor families
Solvent accessibility of the chromophore pocket correlates with adduct-state lifetime.
Our results additionally suggest a correlation between the solvent accessibility of the chromophore pocket and adduct-state lifetime.
Solvent accessibility of the chromophore pocket correlates with adduct-state lifetime.
Our results additionally suggest a correlation between the solvent accessibility of the chromophore pocket and adduct-state lifetime.
Solvent accessibility of the chromophore pocket correlates with adduct-state lifetime.
Our results additionally suggest a correlation between the solvent accessibility of the chromophore pocket and adduct-state lifetime.
Solvent accessibility of the chromophore pocket correlates with adduct-state lifetime.
Our results additionally suggest a correlation between the solvent accessibility of the chromophore pocket and adduct-state lifetime.
Solvent accessibility of the chromophore pocket correlates with adduct-state lifetime.
Our results additionally suggest a correlation between the solvent accessibility of the chromophore pocket and adduct-state lifetime.
Solvent accessibility of the chromophore pocket correlates with adduct-state lifetime.
Our results additionally suggest a correlation between the solvent accessibility of the chromophore pocket and adduct-state lifetime.
Solvent accessibility of the chromophore pocket correlates with adduct-state lifetime.
Our results additionally suggest a correlation between the solvent accessibility of the chromophore pocket and adduct-state lifetime.
PpSB1-LOV is a slow-cycling homologous LOV protein with adduct-state recovery time of 2467 min at 20 b0C.
a slow-cycling (c4rec 2467 min, 20 b0C) homologous protein PpSB1-LOV
adduct-state recovery time 2467 min
PpSB1-LOV is a slow-cycling homologous LOV protein with adduct-state recovery time of 2467 min at 20 b0C.
a slow-cycling (c4rec 2467 min, 20 b0C) homologous protein PpSB1-LOV
adduct-state recovery time 2467 min
PpSB1-LOV is a slow-cycling homologous LOV protein with adduct-state recovery time of 2467 min at 20 b0C.
a slow-cycling (c4rec 2467 min, 20 b0C) homologous protein PpSB1-LOV
adduct-state recovery time 2467 min
PpSB1-LOV is a slow-cycling homologous LOV protein with adduct-state recovery time of 2467 min at 20 b0C.
a slow-cycling (c4rec 2467 min, 20 b0C) homologous protein PpSB1-LOV
adduct-state recovery time 2467 min
PpSB1-LOV is a slow-cycling homologous LOV protein with adduct-state recovery time of 2467 min at 20 b0C.
a slow-cycling (c4rec 2467 min, 20 b0C) homologous protein PpSB1-LOV
adduct-state recovery time 2467 min
PpSB1-LOV is a slow-cycling homologous LOV protein with adduct-state recovery time of 2467 min at 20 b0C.
a slow-cycling (c4rec 2467 min, 20 b0C) homologous protein PpSB1-LOV
adduct-state recovery time 2467 min
PpSB1-LOV is a slow-cycling homologous LOV protein with adduct-state recovery time of 2467 min at 20 b0C.
a slow-cycling (c4rec 2467 min, 20 b0C) homologous protein PpSB1-LOV
adduct-state recovery time 2467 min
PpSB2-LOV is a fast-cycling LOV protein with adduct-state recovery time of 3.5 min at 20 b0C.
we selected PpSB2-LOV, a fast-cycling (c4rec 3.5 min, 20 b0C) short LOV protein
adduct-state recovery time 3.5 min
PpSB2-LOV is a fast-cycling LOV protein with adduct-state recovery time of 3.5 min at 20 b0C.
we selected PpSB2-LOV, a fast-cycling (c4rec 3.5 min, 20 b0C) short LOV protein
adduct-state recovery time 3.5 min
PpSB2-LOV is a fast-cycling LOV protein with adduct-state recovery time of 3.5 min at 20 b0C.
we selected PpSB2-LOV, a fast-cycling (c4rec 3.5 min, 20 b0C) short LOV protein
adduct-state recovery time 3.5 min
PpSB2-LOV is a fast-cycling LOV protein with adduct-state recovery time of 3.5 min at 20 b0C.
we selected PpSB2-LOV, a fast-cycling (c4rec 3.5 min, 20 b0C) short LOV protein
adduct-state recovery time 3.5 min
PpSB2-LOV is a fast-cycling LOV protein with adduct-state recovery time of 3.5 min at 20 b0C.
we selected PpSB2-LOV, a fast-cycling (c4rec 3.5 min, 20 b0C) short LOV protein
adduct-state recovery time 3.5 min
PpSB2-LOV is a fast-cycling LOV protein with adduct-state recovery time of 3.5 min at 20 b0C.
we selected PpSB2-LOV, a fast-cycling (c4rec 3.5 min, 20 b0C) short LOV protein
adduct-state recovery time 3.5 min
PpSB2-LOV is a fast-cycling LOV protein with adduct-state recovery time of 3.5 min at 20 b0C.
we selected PpSB2-LOV, a fast-cycling (c4rec 3.5 min, 20 b0C) short LOV protein
adduct-state recovery time 3.5 min
PpSB2-LOV shares 67% sequence identity with homologous protein PpSB1-LOV.
PpSB2-LOV, a fast-cycling ... protein from Pseudomonas putida that shares 67% sequence identity with a slow-cycling ... homologous protein PpSB1-LOV
sequence identity 67 %
PpSB2-LOV shares 67% sequence identity with homologous protein PpSB1-LOV.
PpSB2-LOV, a fast-cycling ... protein from Pseudomonas putida that shares 67% sequence identity with a slow-cycling ... homologous protein PpSB1-LOV
sequence identity 67 %
PpSB2-LOV shares 67% sequence identity with homologous protein PpSB1-LOV.
PpSB2-LOV, a fast-cycling ... protein from Pseudomonas putida that shares 67% sequence identity with a slow-cycling ... homologous protein PpSB1-LOV
sequence identity 67 %
PpSB2-LOV shares 67% sequence identity with homologous protein PpSB1-LOV.
PpSB2-LOV, a fast-cycling ... protein from Pseudomonas putida that shares 67% sequence identity with a slow-cycling ... homologous protein PpSB1-LOV
sequence identity 67 %
PpSB2-LOV shares 67% sequence identity with homologous protein PpSB1-LOV.
PpSB2-LOV, a fast-cycling ... protein from Pseudomonas putida that shares 67% sequence identity with a slow-cycling ... homologous protein PpSB1-LOV
sequence identity 67 %
PpSB2-LOV shares 67% sequence identity with homologous protein PpSB1-LOV.
PpSB2-LOV, a fast-cycling ... protein from Pseudomonas putida that shares 67% sequence identity with a slow-cycling ... homologous protein PpSB1-LOV
sequence identity 67 %
PpSB2-LOV shares 67% sequence identity with homologous protein PpSB1-LOV.
PpSB2-LOV, a fast-cycling ... protein from Pseudomonas putida that shares 67% sequence identity with a slow-cycling ... homologous protein PpSB1-LOV
sequence identity 67 %
Key amino acids on the Ab2-Bb2 and Eb1-Fb1 loops and the Fb1 helix, including E27 and I66, play a decisive role in determining adduct lifetime in PpSB2-LOV/PpSB1-LOV comparison.
Collectively, the data presented identify key amino acids on the Ab2-Bb2, Eb1-Fb1 loops, and the Fb1 helix, such as E27 and I66, that play a decisive role in determining the adduct lifetime.
Key amino acids on the Ab2-Bb2 and Eb1-Fb1 loops and the Fb1 helix, including E27 and I66, play a decisive role in determining adduct lifetime in PpSB2-LOV/PpSB1-LOV comparison.
Collectively, the data presented identify key amino acids on the Ab2-Bb2, Eb1-Fb1 loops, and the Fb1 helix, such as E27 and I66, that play a decisive role in determining the adduct lifetime.
Key amino acids on the Ab2-Bb2 and Eb1-Fb1 loops and the Fb1 helix, including E27 and I66, play a decisive role in determining adduct lifetime in PpSB2-LOV/PpSB1-LOV comparison.
Collectively, the data presented identify key amino acids on the Ab2-Bb2, Eb1-Fb1 loops, and the Fb1 helix, such as E27 and I66, that play a decisive role in determining the adduct lifetime.
Key amino acids on the Ab2-Bb2 and Eb1-Fb1 loops and the Fb1 helix, including E27 and I66, play a decisive role in determining adduct lifetime in PpSB2-LOV/PpSB1-LOV comparison.
Collectively, the data presented identify key amino acids on the Ab2-Bb2, Eb1-Fb1 loops, and the Fb1 helix, such as E27 and I66, that play a decisive role in determining the adduct lifetime.
Key amino acids on the Ab2-Bb2 and Eb1-Fb1 loops and the Fb1 helix, including E27 and I66, play a decisive role in determining adduct lifetime in PpSB2-LOV/PpSB1-LOV comparison.
Collectively, the data presented identify key amino acids on the Ab2-Bb2, Eb1-Fb1 loops, and the Fb1 helix, such as E27 and I66, that play a decisive role in determining the adduct lifetime.
Key amino acids on the Ab2-Bb2 and Eb1-Fb1 loops and the Fb1 helix, including E27 and I66, play a decisive role in determining adduct lifetime in PpSB2-LOV/PpSB1-LOV comparison.
Collectively, the data presented identify key amino acids on the Ab2-Bb2, Eb1-Fb1 loops, and the Fb1 helix, such as E27 and I66, that play a decisive role in determining the adduct lifetime.
Key amino acids on the Ab2-Bb2 and Eb1-Fb1 loops and the Fb1 helix, including E27 and I66, play a decisive role in determining adduct lifetime in PpSB2-LOV/PpSB1-LOV comparison.
Collectively, the data presented identify key amino acids on the Ab2-Bb2, Eb1-Fb1 loops, and the Fb1 helix, such as E27 and I66, that play a decisive role in determining the adduct lifetime.
Fast- and slow-reverting short LOV proteins similar to PpSB1-LOV and PpSB2-LOV are conserved in different Pseudomonas species.
We now present evidence of the conservation of similar fast and slow-reverting "short" LOV proteins in different Pseudomonas species.
Fast- and slow-reverting short LOV proteins similar to PpSB1-LOV and PpSB2-LOV are conserved in different Pseudomonas species.
We now present evidence of the conservation of similar fast and slow-reverting "short" LOV proteins in different Pseudomonas species.
Fast- and slow-reverting short LOV proteins similar to PpSB1-LOV and PpSB2-LOV are conserved in different Pseudomonas species.
We now present evidence of the conservation of similar fast and slow-reverting "short" LOV proteins in different Pseudomonas species.
Fast- and slow-reverting short LOV proteins similar to PpSB1-LOV and PpSB2-LOV are conserved in different Pseudomonas species.
We now present evidence of the conservation of similar fast and slow-reverting "short" LOV proteins in different Pseudomonas species.
Fast- and slow-reverting short LOV proteins similar to PpSB1-LOV and PpSB2-LOV are conserved in different Pseudomonas species.
We now present evidence of the conservation of similar fast and slow-reverting "short" LOV proteins in different Pseudomonas species.
Fast- and slow-reverting short LOV proteins similar to PpSB1-LOV and PpSB2-LOV are conserved in different Pseudomonas species.
We now present evidence of the conservation of similar fast and slow-reverting "short" LOV proteins in different Pseudomonas species.
Fast- and slow-reverting short LOV proteins similar to PpSB1-LOV and PpSB2-LOV are conserved in different Pseudomonas species.
We now present evidence of the conservation of similar fast and slow-reverting "short" LOV proteins in different Pseudomonas species.
Fast- and slow-reverting short LOV proteins similar to PpSB1-LOV and PpSB2-LOV are conserved in different Pseudomonas species.
We now present evidence of the conservation of similar fast and slow-reverting "short" LOV proteins in different Pseudomonas species.
Fast- and slow-reverting short LOV proteins similar to PpSB1-LOV and PpSB2-LOV are conserved in different Pseudomonas species.
We now present evidence of the conservation of similar fast and slow-reverting "short" LOV proteins in different Pseudomonas species.
PpSB1-LOV and PpSB2-LOV have adduct state lifetimes that vary by 3 orders of magnitude.
PpSB1-LOV and PpSB2-LOV from Pseudomonas putida KT2440 whose adduct state lifetimes varied by 3 orders of magnitude
adduct state lifetime difference 3 orders of magnitude
PpSB1-LOV and PpSB2-LOV have adduct state lifetimes that vary by 3 orders of magnitude.
PpSB1-LOV and PpSB2-LOV from Pseudomonas putida KT2440 whose adduct state lifetimes varied by 3 orders of magnitude
adduct state lifetime difference 3 orders of magnitude
PpSB1-LOV and PpSB2-LOV have adduct state lifetimes that vary by 3 orders of magnitude.
PpSB1-LOV and PpSB2-LOV from Pseudomonas putida KT2440 whose adduct state lifetimes varied by 3 orders of magnitude
adduct state lifetime difference 3 orders of magnitude
PpSB1-LOV and PpSB2-LOV have adduct state lifetimes that vary by 3 orders of magnitude.
PpSB1-LOV and PpSB2-LOV from Pseudomonas putida KT2440 whose adduct state lifetimes varied by 3 orders of magnitude
adduct state lifetime difference 3 orders of magnitude
PpSB1-LOV and PpSB2-LOV have adduct state lifetimes that vary by 3 orders of magnitude.
PpSB1-LOV and PpSB2-LOV from Pseudomonas putida KT2440 whose adduct state lifetimes varied by 3 orders of magnitude
adduct state lifetime difference 3 orders of magnitude
PpSB1-LOV and PpSB2-LOV have adduct state lifetimes that vary by 3 orders of magnitude.
PpSB1-LOV and PpSB2-LOV from Pseudomonas putida KT2440 whose adduct state lifetimes varied by 3 orders of magnitude
adduct state lifetime difference 3 orders of magnitude
PpSB1-LOV and PpSB2-LOV have adduct state lifetimes that vary by 3 orders of magnitude.
PpSB1-LOV and PpSB2-LOV from Pseudomonas putida KT2440 whose adduct state lifetimes varied by 3 orders of magnitude
adduct state lifetime difference 3 orders of magnitude
PpSB1-LOV and PpSB2-LOV have adduct state lifetimes that vary by 3 orders of magnitude.
PpSB1-LOV and PpSB2-LOV from Pseudomonas putida KT2440 whose adduct state lifetimes varied by 3 orders of magnitude
adduct state lifetime difference 3 orders of magnitude
PpSB1-LOV and PpSB2-LOV have adduct state lifetimes that vary by 3 orders of magnitude.
PpSB1-LOV and PpSB2-LOV from Pseudomonas putida KT2440 whose adduct state lifetimes varied by 3 orders of magnitude
adduct state lifetime difference 3 orders of magnitude
The short C-terminal extensions of PpSB1-LOV and PpSB2-LOV form independently folding helical structures in solution.
circular dichroism and solution nuclear magnetic resonance experiments verify that the two short C-terminal extensions of PpSB1-LOV and PpSB2-LOV form independently folding helical structures in solution
The short C-terminal extensions of PpSB1-LOV and PpSB2-LOV form independently folding helical structures in solution.
circular dichroism and solution nuclear magnetic resonance experiments verify that the two short C-terminal extensions of PpSB1-LOV and PpSB2-LOV form independently folding helical structures in solution
The short C-terminal extensions of PpSB1-LOV and PpSB2-LOV form independently folding helical structures in solution.
circular dichroism and solution nuclear magnetic resonance experiments verify that the two short C-terminal extensions of PpSB1-LOV and PpSB2-LOV form independently folding helical structures in solution
The short C-terminal extensions of PpSB1-LOV and PpSB2-LOV form independently folding helical structures in solution.
circular dichroism and solution nuclear magnetic resonance experiments verify that the two short C-terminal extensions of PpSB1-LOV and PpSB2-LOV form independently folding helical structures in solution
The short C-terminal extensions of PpSB1-LOV and PpSB2-LOV form independently folding helical structures in solution.
circular dichroism and solution nuclear magnetic resonance experiments verify that the two short C-terminal extensions of PpSB1-LOV and PpSB2-LOV form independently folding helical structures in solution
The short C-terminal extensions of PpSB1-LOV and PpSB2-LOV form independently folding helical structures in solution.
circular dichroism and solution nuclear magnetic resonance experiments verify that the two short C-terminal extensions of PpSB1-LOV and PpSB2-LOV form independently folding helical structures in solution
The short C-terminal extensions of PpSB1-LOV and PpSB2-LOV form independently folding helical structures in solution.
circular dichroism and solution nuclear magnetic resonance experiments verify that the two short C-terminal extensions of PpSB1-LOV and PpSB2-LOV form independently folding helical structures in solution
The short C-terminal extensions of PpSB1-LOV and PpSB2-LOV form independently folding helical structures in solution.
circular dichroism and solution nuclear magnetic resonance experiments verify that the two short C-terminal extensions of PpSB1-LOV and PpSB2-LOV form independently folding helical structures in solution
The short C-terminal extensions of PpSB1-LOV and PpSB2-LOV form independently folding helical structures in solution.
circular dichroism and solution nuclear magnetic resonance experiments verify that the two short C-terminal extensions of PpSB1-LOV and PpSB2-LOV form independently folding helical structures in solution
Bioinformatic analyses imply that the structural elements corresponding to the short C-terminal extensions form coiled coils in the context of the dimeric full-length proteins.
bioinformatic analyses imply the formation of coiled coils of the respective structural elements in the context of the dimeric full-length proteins
Bioinformatic analyses imply that the structural elements corresponding to the short C-terminal extensions form coiled coils in the context of the dimeric full-length proteins.
bioinformatic analyses imply the formation of coiled coils of the respective structural elements in the context of the dimeric full-length proteins
Bioinformatic analyses imply that the structural elements corresponding to the short C-terminal extensions form coiled coils in the context of the dimeric full-length proteins.
bioinformatic analyses imply the formation of coiled coils of the respective structural elements in the context of the dimeric full-length proteins
Bioinformatic analyses imply that the structural elements corresponding to the short C-terminal extensions form coiled coils in the context of the dimeric full-length proteins.
bioinformatic analyses imply the formation of coiled coils of the respective structural elements in the context of the dimeric full-length proteins
Bioinformatic analyses imply that the structural elements corresponding to the short C-terminal extensions form coiled coils in the context of the dimeric full-length proteins.
bioinformatic analyses imply the formation of coiled coils of the respective structural elements in the context of the dimeric full-length proteins
Bioinformatic analyses imply that the structural elements corresponding to the short C-terminal extensions form coiled coils in the context of the dimeric full-length proteins.
bioinformatic analyses imply the formation of coiled coils of the respective structural elements in the context of the dimeric full-length proteins
Bioinformatic analyses imply that the structural elements corresponding to the short C-terminal extensions form coiled coils in the context of the dimeric full-length proteins.
bioinformatic analyses imply the formation of coiled coils of the respective structural elements in the context of the dimeric full-length proteins
Bioinformatic analyses imply that the structural elements corresponding to the short C-terminal extensions form coiled coils in the context of the dimeric full-length proteins.
bioinformatic analyses imply the formation of coiled coils of the respective structural elements in the context of the dimeric full-length proteins
Bioinformatic analyses imply that the structural elements corresponding to the short C-terminal extensions form coiled coils in the context of the dimeric full-length proteins.
bioinformatic analyses imply the formation of coiled coils of the respective structural elements in the context of the dimeric full-length proteins
The short N- and C-terminal extensions outside the LOV core domain are essential for the structural integrity and folding of PpSB1-LOV and PpSB2-LOV.
Truncation studies conducted with PpSB1-LOV and PpSB2-LOV suggested that the short N- and C-terminal extensions outside of the LOV core domain are essential for the structural integrity and folding of the two proteins.
The short N- and C-terminal extensions outside the LOV core domain are essential for the structural integrity and folding of PpSB1-LOV and PpSB2-LOV.
Truncation studies conducted with PpSB1-LOV and PpSB2-LOV suggested that the short N- and C-terminal extensions outside of the LOV core domain are essential for the structural integrity and folding of the two proteins.
The short N- and C-terminal extensions outside the LOV core domain are essential for the structural integrity and folding of PpSB1-LOV and PpSB2-LOV.
Truncation studies conducted with PpSB1-LOV and PpSB2-LOV suggested that the short N- and C-terminal extensions outside of the LOV core domain are essential for the structural integrity and folding of the two proteins.
The short N- and C-terminal extensions outside the LOV core domain are essential for the structural integrity and folding of PpSB1-LOV and PpSB2-LOV.
Truncation studies conducted with PpSB1-LOV and PpSB2-LOV suggested that the short N- and C-terminal extensions outside of the LOV core domain are essential for the structural integrity and folding of the two proteins.
The short N- and C-terminal extensions outside the LOV core domain are essential for the structural integrity and folding of PpSB1-LOV and PpSB2-LOV.
Truncation studies conducted with PpSB1-LOV and PpSB2-LOV suggested that the short N- and C-terminal extensions outside of the LOV core domain are essential for the structural integrity and folding of the two proteins.
The short N- and C-terminal extensions outside the LOV core domain are essential for the structural integrity and folding of PpSB1-LOV and PpSB2-LOV.
Truncation studies conducted with PpSB1-LOV and PpSB2-LOV suggested that the short N- and C-terminal extensions outside of the LOV core domain are essential for the structural integrity and folding of the two proteins.
The short N- and C-terminal extensions outside the LOV core domain are essential for the structural integrity and folding of PpSB1-LOV and PpSB2-LOV.
Truncation studies conducted with PpSB1-LOV and PpSB2-LOV suggested that the short N- and C-terminal extensions outside of the LOV core domain are essential for the structural integrity and folding of the two proteins.
The short N- and C-terminal extensions outside the LOV core domain are essential for the structural integrity and folding of PpSB1-LOV and PpSB2-LOV.
Truncation studies conducted with PpSB1-LOV and PpSB2-LOV suggested that the short N- and C-terminal extensions outside of the LOV core domain are essential for the structural integrity and folding of the two proteins.
The short N- and C-terminal extensions outside the LOV core domain are essential for the structural integrity and folding of PpSB1-LOV and PpSB2-LOV.
Truncation studies conducted with PpSB1-LOV and PpSB2-LOV suggested that the short N- and C-terminal extensions outside of the LOV core domain are essential for the structural integrity and folding of the two proteins.
Short LOV proteins could be ideally suited building blocks for the design of genetically encoded photoswitches.
Given their prototypic architecture, conserved in most more complex LOV photoreceptor systems, "short" LOV proteins could represent ideally suited building blocks for the design of genetically encoded photoswitches (i.e., LOV-based optogenetic tools).
Short LOV proteins could be ideally suited building blocks for the design of genetically encoded photoswitches.
Given their prototypic architecture, conserved in most more complex LOV photoreceptor systems, "short" LOV proteins could represent ideally suited building blocks for the design of genetically encoded photoswitches (i.e., LOV-based optogenetic tools).
Short LOV proteins could be ideally suited building blocks for the design of genetically encoded photoswitches.
Given their prototypic architecture, conserved in most more complex LOV photoreceptor systems, "short" LOV proteins could represent ideally suited building blocks for the design of genetically encoded photoswitches (i.e., LOV-based optogenetic tools).
Short LOV proteins could be ideally suited building blocks for the design of genetically encoded photoswitches.
Given their prototypic architecture, conserved in most more complex LOV photoreceptor systems, "short" LOV proteins could represent ideally suited building blocks for the design of genetically encoded photoswitches (i.e., LOV-based optogenetic tools).
Short LOV proteins could be ideally suited building blocks for the design of genetically encoded photoswitches.
Given their prototypic architecture, conserved in most more complex LOV photoreceptor systems, "short" LOV proteins could represent ideally suited building blocks for the design of genetically encoded photoswitches (i.e., LOV-based optogenetic tools).
Short LOV proteins could be ideally suited building blocks for the design of genetically encoded photoswitches.
Given their prototypic architecture, conserved in most more complex LOV photoreceptor systems, "short" LOV proteins could represent ideally suited building blocks for the design of genetically encoded photoswitches (i.e., LOV-based optogenetic tools).
Short LOV proteins could be ideally suited building blocks for the design of genetically encoded photoswitches.
Given their prototypic architecture, conserved in most more complex LOV photoreceptor systems, "short" LOV proteins could represent ideally suited building blocks for the design of genetically encoded photoswitches (i.e., LOV-based optogenetic tools).
Short LOV proteins could be ideally suited building blocks for the design of genetically encoded photoswitches.
Given their prototypic architecture, conserved in most more complex LOV photoreceptor systems, "short" LOV proteins could represent ideally suited building blocks for the design of genetically encoded photoswitches (i.e., LOV-based optogenetic tools).
Short LOV proteins could be ideally suited building blocks for the design of genetically encoded photoswitches.
Given their prototypic architecture, conserved in most more complex LOV photoreceptor systems, "short" LOV proteins could represent ideally suited building blocks for the design of genetically encoded photoswitches (i.e., LOV-based optogenetic tools).
Approval Evidence
3 sources13 linked approval claimsfirst-pass slug ppsb1-lov
Using the slow cycling bacterial short LOV photoreceptor PpSB1-LOV, we show that the I48T mutation within this pocket, which accelerates adduct rupture, is otherwise structurally and mechanistically benign
Source:
a slow-cycling (c4rec 2467 min, 20 b0C) homologous protein PpSB1-LOV
Source:
We recently described the slow and fast reverting "short" LOV proteins PpSB1-LOV and PpSB2-LOV from Pseudomonas putida KT2440 whose adduct state lifetimes varied by 3 orders of magnitude
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application potentialsupports
The identified conserved-pocket mutations should find application in dark-recovery tuning of optogenetic tools and LOV photoreceptors.
Given the conserved nature of the corresponding structural region, the here identified mutations should find application in dark-recovery tuning of optogenetic tools and LOV photoreceptors, alike.
Source:
cross family generalizationsupports
Additional pocket mutations in PpSB1-LOV and homologous mutations in YtvA and the Avena sativa LOV2 domain produce similarly altered kinetics.
Additional mutations within the pocket of PpSB1-LOV and the introduction of homologous mutations in the LOV photoreceptor YtvA of Bacillus subtilis and the Avena sativa LOV2 domain result in similarly altered kinetics.
Source:
mutation effectsupports
In PpSB1-LOV, the I48T mutation accelerates adduct rupture and is structurally and mechanistically benign, with unaltered light-induced structural changes by NMR spectroscopy and X-ray crystallography.
Using the slow cycling bacterial short LOV photoreceptor PpSB1-LOV, we show that the I48T mutation within this pocket, which accelerates adduct rupture, is otherwise structurally and mechanistically benign, i.e., light-induced structural changes, as probed by NMR spectroscopy and X-ray crystallography, are not altered in the variant.
Source:
correlationsupports
Solvent accessibility of the chromophore pocket correlates with adduct-state lifetime.
Our results additionally suggest a correlation between the solvent accessibility of the chromophore pocket and adduct-state lifetime.
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kinetic propertysupports
PpSB1-LOV is a slow-cycling homologous LOV protein with adduct-state recovery time of 2467 min at 20 b0C.
a slow-cycling (c4rec 2467 min, 20 b0C) homologous protein PpSB1-LOV
Source:
sequence similaritysupports
PpSB2-LOV shares 67% sequence identity with homologous protein PpSB1-LOV.
PpSB2-LOV, a fast-cycling ... protein from Pseudomonas putida that shares 67% sequence identity with a slow-cycling ... homologous protein PpSB1-LOV
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structure function relationshipsupports
Key amino acids on the Ab2-Bb2 and Eb1-Fb1 loops and the Fb1 helix, including E27 and I66, play a decisive role in determining adduct lifetime in PpSB2-LOV/PpSB1-LOV comparison.
Collectively, the data presented identify key amino acids on the Ab2-Bb2, Eb1-Fb1 loops, and the Fb1 helix, such as E27 and I66, that play a decisive role in determining the adduct lifetime.
Source:
conservationsupports
Fast- and slow-reverting short LOV proteins similar to PpSB1-LOV and PpSB2-LOV are conserved in different Pseudomonas species.
We now present evidence of the conservation of similar fast and slow-reverting "short" LOV proteins in different Pseudomonas species.
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kinetic diversitysupports
PpSB1-LOV and PpSB2-LOV have adduct state lifetimes that vary by 3 orders of magnitude.
PpSB1-LOV and PpSB2-LOV from Pseudomonas putida KT2440 whose adduct state lifetimes varied by 3 orders of magnitude
Source:
structural featuresupports
The short C-terminal extensions of PpSB1-LOV and PpSB2-LOV form independently folding helical structures in solution.
circular dichroism and solution nuclear magnetic resonance experiments verify that the two short C-terminal extensions of PpSB1-LOV and PpSB2-LOV form independently folding helical structures in solution
Source:
structural inferencesupports
Bioinformatic analyses imply that the structural elements corresponding to the short C-terminal extensions form coiled coils in the context of the dimeric full-length proteins.
bioinformatic analyses imply the formation of coiled coils of the respective structural elements in the context of the dimeric full-length proteins
Source:
structure functionsupports
The short N- and C-terminal extensions outside the LOV core domain are essential for the structural integrity and folding of PpSB1-LOV and PpSB2-LOV.
Truncation studies conducted with PpSB1-LOV and PpSB2-LOV suggested that the short N- and C-terminal extensions outside of the LOV core domain are essential for the structural integrity and folding of the two proteins.
Source:
tool design implicationsupports
Short LOV proteins could be ideally suited building blocks for the design of genetically encoded photoswitches.
Given their prototypic architecture, conserved in most more complex LOV photoreceptor systems, "short" LOV proteins could represent ideally suited building blocks for the design of genetically encoded photoswitches (i.e., LOV-based optogenetic tools).
Source:
Comparisons
Source-backed strengths
PpSB1-LOV is reported to be a slow-cycling short LOV protein with a dark recovery time of about 2467 min at 20 °C, and its adduct-state lifetime differs from the related PpSB2-LOV by roughly 3 orders of magnitude. The I48T conserved-pocket mutation accelerates adduct rupture without detectable disruption of the domain's light-induced structural changes, supporting its use as a tunable yet mechanistically intact scaffold.
Source:
part of a pair whose adduct state lifetimes varied by 3 orders of magnitude
Source:
short C-terminal extension forms an independently folding helical structure in solution
Ranked Citations
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