Source 1primary paper2013Biochemistry
Toolkit/PpSB2-LOV
PpSB2-LOV
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
PpSB2-LOV is a compact "short" light, oxygen, voltage (LOV) photosensory protein from Pseudomonas putida KT2440. It forms a light-induced LOV photoadduct and exhibits rapid dark-state thermal recovery, with a reported recovery time of 3.5 min at 20 °C, making it a candidate building block for genetically encoded photoswitches.
Usefulness & Problems
Why this is useful
PpSB2-LOV is useful as a small LOV-domain module with defined and rapid recovery kinetics for engineering light-responsive proteins. Its strong kinetic contrast with the homologous PpSB1-LOV, whose adduct-state lifetime differs by roughly three orders of magnitude, supports its value for tuning photoswitch timing.
Source:
PpSB2-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 tool helps address the need for compact photosensory domains with characterized photocycle kinetics for optogenetic and photoswitch design. The available evidence supports its role as a candidate module for controlling recovery times, but not as a complete validated switch in a target cellular system.
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 thermal recoveryHeterodimerizationphotoadduct formationphotoadduct formation and dark-state thermal recoveryTarget processes
No target processes tagged yet.
Input: Light
Implementation Constraints
The literature describes PpSB2-LOV as a short LOV protein from Pseudomonas putida KT2440 and notes that intact N- and C-terminal extensions appear important for proper folding and structural integrity. Structural characterization and truncation-related assessments are referenced, but the supplied evidence does not provide construct sequences, expression conditions, or cofactor-handling details.
The supplied evidence does not demonstrate PpSB2-LOV functioning as a standalone optogenetic actuator or regulator in cells. Evidence for heterodimerization is listed in the metadata, but the provided source excerpts do not substantiate that mechanism for PpSB2-LOV specifically.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2primary paper2021FEBS Journal
Ranked Claims
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
2 sources10 linked approval claimsfirst-pass slug ppsb2-lov
we selected PpSB2-LOV, a fast-cycling (c4rec 3.5 min, 20 b0C) short LOV protein from Pseudomonas putida
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
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
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
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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.
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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
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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
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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
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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.
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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).
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Comparisons
Source-backed strengths
PpSB2-LOV is explicitly described as a fast-cycling short LOV protein with an adduct-state recovery time of 3.5 min at 20 °C. Comparative studies with PpSB1-LOV indicate that closely related Pseudomonas putida LOV proteins can differ in adduct lifetime by three orders of magnitude, and structural analysis linked chromophore-pocket solvent accessibility to adduct-state lifetime.
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part of a pair whose adduct state lifetimes varied by 3 orders of magnitude
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short C-terminal extension forms an independently folding helical structure in solution
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