Source 1primary paper2013Acta Crystallographica Section F Structural Biology and Crystallization Communications
Toolkit/phototropin 1 LOV2 domain
phototropin 1 LOV2 domain
Also known as: A. thaliana phototropin 1 LOV2 domain, LOV2 domain, LOV2 domain of phot1
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The Arabidopsis thaliana phototropin 1 LOV2 domain is a blue-light-sensing protein domain from phototropin 1 whose dark-adapted crystal structure has been determined. In this state, the domain is dimeric and contains an N-terminal A'α helix and a C-terminal Jα helix that contribute to coiled-coil-mediated dimerization.
Usefulness & Problems
Why this is useful
This domain is useful as a structurally characterized blue-light-responsive module from a native plant photoreceptor. The available evidence supports its relevance for studying light sensing, dimerization, phototropism, and leaf expansion, but does not provide direct tool-performance data in engineered systems.
Source:
The Jα helix predominantly interacts with the β-sheet and plays a role in coiled-coil formation and dimerization.
Source:
Our results show that the LOV2 domain of phot1 plays a major role in phototropism and leaf expansion
Source:
as does the LOV2 domain of phot2
Problem solved
It helps address the problem of obtaining a defined blue-light-sensing protein domain with resolved dark-state architecture and a characterized dimer interface. The evidence also links the phot1 LOV2 domain to physiological light responses in Arabidopsis thaliana, specifically phototropism and leaf expansion.
Problem links
Need precise spatiotemporal control with light input
DerivedThe Arabidopsis thaliana phototropin 1 LOV2 domain is a blue-light-sensing protein domain whose dark-adapted crystal structure has been determined. In phot1, this LOV2 domain forms a dimer with a coiled-coil interface involving the N-terminal A'α helices and is reported to play a major role in phototropism and leaf expansion.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
coiled-coil-mediated associationdimerizationHeterodimerizationHeterodimerizationlight sensingTarget processes
No target processes tagged yet.
Input: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenimplementation constraint: spectral hardware requirementoperating role: actuatorswitch architecture: multi componentswitch architecture: recruitment
The structurally characterized state is the dark-adapted form of the Arabidopsis thaliana phot1 LOV2 domain. Construct features supported by the evidence include the LOV2 core flanked by an N-terminal A'α helix and a C-terminal Jα helix, with both helices contributing to dimerization-related architecture. No explicit expression system, delivery strategy, or engineering design rules are described in the supplied evidence.
The supplied evidence is limited mainly to structural characterization and qualitative functional association in Arabidopsis. No quantitative photochemical parameters, kinetics, cofactor requirements, spectral values, mutational optimization, or validation in heterologous engineered applications are provided.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2primary paper2006PLANT PHYSIOLOGY
Ranked Claims
In Arabidopsis thaliana phototropin 1 LOV2, two A'α helices adopt a scissor-like orientation at the dimer interface and form a short α-helical coiled coil.
two A'α helices adopt a scissor-like orientation at the dimer interface and form a short α-helical coiled coil
In Arabidopsis thaliana phototropin 1 LOV2, two A'α helices adopt a scissor-like orientation at the dimer interface and form a short α-helical coiled coil.
two A'α helices adopt a scissor-like orientation at the dimer interface and form a short α-helical coiled coil
In Arabidopsis thaliana phototropin 1 LOV2, two A'α helices adopt a scissor-like orientation at the dimer interface and form a short α-helical coiled coil.
two A'α helices adopt a scissor-like orientation at the dimer interface and form a short α-helical coiled coil
In Arabidopsis thaliana phototropin 1 LOV2, two A'α helices adopt a scissor-like orientation at the dimer interface and form a short α-helical coiled coil.
two A'α helices adopt a scissor-like orientation at the dimer interface and form a short α-helical coiled coil
In Arabidopsis thaliana phototropin 1 LOV2, two A'α helices adopt a scissor-like orientation at the dimer interface and form a short α-helical coiled coil.
two A'α helices adopt a scissor-like orientation at the dimer interface and form a short α-helical coiled coil
In Arabidopsis thaliana phototropin 1 LOV2, two A'α helices adopt a scissor-like orientation at the dimer interface and form a short α-helical coiled coil.
two A'α helices adopt a scissor-like orientation at the dimer interface and form a short α-helical coiled coil
The Jα helix predominantly interacts with the β-sheet and plays a role in coiled-coil formation and dimerization.
The Jα helix predominantly interacts with the β-sheet and plays a role in coiled-coil formation and dimerization.
The Jα helix predominantly interacts with the β-sheet and plays a role in coiled-coil formation and dimerization.
The Jα helix predominantly interacts with the β-sheet and plays a role in coiled-coil formation and dimerization.
The Jα helix predominantly interacts with the β-sheet and plays a role in coiled-coil formation and dimerization.
The Jα helix predominantly interacts with the β-sheet and plays a role in coiled-coil formation and dimerization.
The Jα helix predominantly interacts with the β-sheet and plays a role in coiled-coil formation and dimerization.
The Jα helix predominantly interacts with the β-sheet and plays a role in coiled-coil formation and dimerization.
The Jα helix predominantly interacts with the β-sheet and plays a role in coiled-coil formation and dimerization.
The Jα helix predominantly interacts with the β-sheet and plays a role in coiled-coil formation and dimerization.
The Jα helix predominantly interacts with the β-sheet and plays a role in coiled-coil formation and dimerization.
The Jα helix predominantly interacts with the β-sheet and plays a role in coiled-coil formation and dimerization.
Arabidopsis thaliana phototropin 1 LOV2 is a dimer, unlike the monomeric Avena sativa LOV2.
In contrast to the monomeric A. sativa LOV2, A. thaliana LOV2 is a dimer
Arabidopsis thaliana phototropin 1 LOV2 is a dimer, unlike the monomeric Avena sativa LOV2.
In contrast to the monomeric A. sativa LOV2, A. thaliana LOV2 is a dimer
Arabidopsis thaliana phototropin 1 LOV2 is a dimer, unlike the monomeric Avena sativa LOV2.
In contrast to the monomeric A. sativa LOV2, A. thaliana LOV2 is a dimer
Arabidopsis thaliana phototropin 1 LOV2 is a dimer, unlike the monomeric Avena sativa LOV2.
In contrast to the monomeric A. sativa LOV2, A. thaliana LOV2 is a dimer
Arabidopsis thaliana phototropin 1 LOV2 is a dimer, unlike the monomeric Avena sativa LOV2.
In contrast to the monomeric A. sativa LOV2, A. thaliana LOV2 is a dimer
Arabidopsis thaliana phototropin 1 LOV2 is a dimer, unlike the monomeric Avena sativa LOV2.
In contrast to the monomeric A. sativa LOV2, A. thaliana LOV2 is a dimer
The crystal structure of the Arabidopsis thaliana phototropin 1 LOV2 domain was determined in the dark-adapted state.
Here, the crystal structure of the A. thaliana phototropin 1 LOV2 domain has been determined in its dark-adapted state.
The crystal structure of the Arabidopsis thaliana phototropin 1 LOV2 domain was determined in the dark-adapted state.
Here, the crystal structure of the A. thaliana phototropin 1 LOV2 domain has been determined in its dark-adapted state.
The crystal structure of the Arabidopsis thaliana phototropin 1 LOV2 domain was determined in the dark-adapted state.
Here, the crystal structure of the A. thaliana phototropin 1 LOV2 domain has been determined in its dark-adapted state.
The crystal structure of the Arabidopsis thaliana phototropin 1 LOV2 domain was determined in the dark-adapted state.
Here, the crystal structure of the A. thaliana phototropin 1 LOV2 domain has been determined in its dark-adapted state.
The crystal structure of the Arabidopsis thaliana phototropin 1 LOV2 domain was determined in the dark-adapted state.
Here, the crystal structure of the A. thaliana phototropin 1 LOV2 domain has been determined in its dark-adapted state.
The crystal structure of the Arabidopsis thaliana phototropin 1 LOV2 domain was determined in the dark-adapted state.
Here, the crystal structure of the A. thaliana phototropin 1 LOV2 domain has been determined in its dark-adapted state.
The Arabidopsis thaliana phototropin 1 LOV2 core is flanked by an N-terminal A'α helix and a C-terminal Jα helix.
The core is flanked by an N-terminal A'α helix and a C-terminal Jα helix
The Arabidopsis thaliana phototropin 1 LOV2 core is flanked by an N-terminal A'α helix and a C-terminal Jα helix.
The core is flanked by an N-terminal A'α helix and a C-terminal Jα helix
The Arabidopsis thaliana phototropin 1 LOV2 core is flanked by an N-terminal A'α helix and a C-terminal Jα helix.
The core is flanked by an N-terminal A'α helix and a C-terminal Jα helix
The Arabidopsis thaliana phototropin 1 LOV2 core is flanked by an N-terminal A'α helix and a C-terminal Jα helix.
The core is flanked by an N-terminal A'α helix and a C-terminal Jα helix
The Arabidopsis thaliana phototropin 1 LOV2 core is flanked by an N-terminal A'α helix and a C-terminal Jα helix.
The core is flanked by an N-terminal A'α helix and a C-terminal Jα helix
The Arabidopsis thaliana phototropin 1 LOV2 core is flanked by an N-terminal A'α helix and a C-terminal Jα helix.
The core is flanked by an N-terminal A'α helix and a C-terminal Jα helix
The LOV1 domain of phototropin 1 did not complement phototropism or leaf expansion.
No complementation of phototropism or leaf expansion was observed for the LOV1 domain of phot1
The LOV1 domain of phototropin 1 did not complement phototropism or leaf expansion.
No complementation of phototropism or leaf expansion was observed for the LOV1 domain of phot1
The LOV1 domain of phototropin 1 did not complement phototropism or leaf expansion.
No complementation of phototropism or leaf expansion was observed for the LOV1 domain of phot1
The LOV1 domain of phototropin 1 did not complement phototropism or leaf expansion.
No complementation of phototropism or leaf expansion was observed for the LOV1 domain of phot1
The LOV1 domain of phototropin 1 did not complement phototropism or leaf expansion.
No complementation of phototropism or leaf expansion was observed for the LOV1 domain of phot1
The LOV1 domain of phototropin 1 did not complement phototropism or leaf expansion.
No complementation of phototropism or leaf expansion was observed for the LOV1 domain of phot1
The LOV1 domain of phototropin 1 did not complement phototropism or leaf expansion.
No complementation of phototropism or leaf expansion was observed for the LOV1 domain of phot1
The LOV1 domain of phototropin 1 did not complement phototropism or leaf expansion.
No complementation of phototropism or leaf expansion was observed for the LOV1 domain of phot1
The LOV1 domain of phototropin 1 did not complement phototropism or leaf expansion.
No complementation of phototropism or leaf expansion was observed for the LOV1 domain of phot1
The LOV1 domain of phototropin 1 did not complement phototropism or leaf expansion.
No complementation of phototropism or leaf expansion was observed for the LOV1 domain of phot1
The LOV1 domain of phototropin 2 complemented phototropism to a considerable level.
phot2 LOV1 was unexpectedly found to complement phototropism to a considerable level
complementation level considerable level
The LOV1 domain of phototropin 2 complemented phototropism to a considerable level.
phot2 LOV1 was unexpectedly found to complement phototropism to a considerable level
complementation level considerable level
The LOV1 domain of phototropin 2 complemented phototropism to a considerable level.
phot2 LOV1 was unexpectedly found to complement phototropism to a considerable level
complementation level considerable level
The LOV1 domain of phototropin 2 complemented phototropism to a considerable level.
phot2 LOV1 was unexpectedly found to complement phototropism to a considerable level
complementation level considerable level
The LOV1 domain of phototropin 2 complemented phototropism to a considerable level.
phot2 LOV1 was unexpectedly found to complement phototropism to a considerable level
complementation level considerable level
The LOV1 domain of phototropin 2 complemented phototropism to a considerable level.
phot2 LOV1 was unexpectedly found to complement phototropism to a considerable level
complementation level considerable level
The LOV1 domain of phototropin 2 complemented phototropism to a considerable level.
phot2 LOV1 was unexpectedly found to complement phototropism to a considerable level
complementation level considerable level
The LOV1 domain of phototropin 2 complemented phototropism to a considerable level.
phot2 LOV1 was unexpectedly found to complement phototropism to a considerable level
complementation level considerable level
The LOV1 domain of phototropin 2 complemented phototropism to a considerable level.
phot2 LOV1 was unexpectedly found to complement phototropism to a considerable level
complementation level considerable level
The LOV1 domain of phototropin 2 complemented phototropism to a considerable level.
phot2 LOV1 was unexpectedly found to complement phototropism to a considerable level
complementation level considerable level
The LOV2 domain of phototropin 1 plays a major role in phototropism and leaf expansion.
Our results show that the LOV2 domain of phot1 plays a major role in phototropism and leaf expansion
The LOV2 domain of phototropin 1 plays a major role in phototropism and leaf expansion.
Our results show that the LOV2 domain of phot1 plays a major role in phototropism and leaf expansion
The LOV2 domain of phototropin 1 plays a major role in phototropism and leaf expansion.
Our results show that the LOV2 domain of phot1 plays a major role in phototropism and leaf expansion
The LOV2 domain of phototropin 1 plays a major role in phototropism and leaf expansion.
Our results show that the LOV2 domain of phot1 plays a major role in phototropism and leaf expansion
The LOV2 domain of phototropin 1 plays a major role in phototropism and leaf expansion.
Our results show that the LOV2 domain of phot1 plays a major role in phototropism and leaf expansion
The LOV2 domain of phototropin 1 plays a major role in phototropism and leaf expansion.
Our results show that the LOV2 domain of phot1 plays a major role in phototropism and leaf expansion
The LOV2 domain of phototropin 1 plays a major role in phototropism and leaf expansion.
Our results show that the LOV2 domain of phot1 plays a major role in phototropism and leaf expansion
The LOV2 domain of phototropin 1 plays a major role in phototropism and leaf expansion.
Our results show that the LOV2 domain of phot1 plays a major role in phototropism and leaf expansion
The LOV2 domain of phototropin 1 plays a major role in phototropism and leaf expansion.
Our results show that the LOV2 domain of phot1 plays a major role in phototropism and leaf expansion
The LOV2 domain of phototropin 1 plays a major role in phototropism and leaf expansion.
Our results show that the LOV2 domain of phot1 plays a major role in phototropism and leaf expansion
The LOV2 domain of phototropin 1 plays a major role in phototropism and leaf expansion.
Our results show that the LOV2 domain of phot1 plays a major role in phototropism and leaf expansion
The LOV2 domain of phototropin 1 plays a major role in phototropism and leaf expansion.
Our results show that the LOV2 domain of phot1 plays a major role in phototropism and leaf expansion
The LOV2 domain of phototropin 1 plays a major role in phototropism and leaf expansion.
Our results show that the LOV2 domain of phot1 plays a major role in phototropism and leaf expansion
The LOV2 domain of phototropin 1 plays a major role in phototropism and leaf expansion.
Our results show that the LOV2 domain of phot1 plays a major role in phototropism and leaf expansion
The LOV2 domain of phototropin 1 plays a major role in phototropism and leaf expansion.
Our results show that the LOV2 domain of phot1 plays a major role in phototropism and leaf expansion
The LOV2 domain of phototropin 1 plays a major role in phototropism and leaf expansion.
Our results show that the LOV2 domain of phot1 plays a major role in phototropism and leaf expansion
The LOV2 domain of phototropin 1 plays a major role in phototropism and leaf expansion.
Our results show that the LOV2 domain of phot1 plays a major role in phototropism and leaf expansion
The LOV2 domain of phototropin 2 plays a major role in phototropism and leaf expansion.
as does the LOV2 domain of phot2
The LOV2 domain of phototropin 2 plays a major role in phototropism and leaf expansion.
as does the LOV2 domain of phot2
The LOV2 domain of phototropin 2 plays a major role in phototropism and leaf expansion.
as does the LOV2 domain of phot2
The LOV2 domain of phototropin 2 plays a major role in phototropism and leaf expansion.
as does the LOV2 domain of phot2
The LOV2 domain of phototropin 2 plays a major role in phototropism and leaf expansion.
as does the LOV2 domain of phot2
The LOV2 domain of phototropin 2 plays a major role in phototropism and leaf expansion.
as does the LOV2 domain of phot2
The LOV2 domain of phototropin 2 plays a major role in phototropism and leaf expansion.
as does the LOV2 domain of phot2
The LOV2 domain of phototropin 2 plays a major role in phototropism and leaf expansion.
as does the LOV2 domain of phot2
The LOV2 domain of phototropin 2 plays a major role in phototropism and leaf expansion.
as does the LOV2 domain of phot2
The LOV2 domain of phototropin 2 plays a major role in phototropism and leaf expansion.
as does the LOV2 domain of phot2
Approval Evidence
2 sources6 linked approval claimsfirst-pass slug phototropin-1-lov2-domain
Here, the crystal structure of the A. thaliana phototropin 1 LOV2 domain has been determined in its dark-adapted state.
Source:
the LOV2 domain of phot1 plays a major role in phototropism and leaf expansion
Source:
dimerization mechanismsupports
In Arabidopsis thaliana phototropin 1 LOV2, two A'α helices adopt a scissor-like orientation at the dimer interface and form a short α-helical coiled coil.
two A'α helices adopt a scissor-like orientation at the dimer interface and form a short α-helical coiled coil
Source:
functional rolesupports
The Jα helix predominantly interacts with the β-sheet and plays a role in coiled-coil formation and dimerization.
The Jα helix predominantly interacts with the β-sheet and plays a role in coiled-coil formation and dimerization.
Source:
oligomeric statesupports
Arabidopsis thaliana phototropin 1 LOV2 is a dimer, unlike the monomeric Avena sativa LOV2.
In contrast to the monomeric A. sativa LOV2, A. thaliana LOV2 is a dimer
Source:
structural characterizationsupports
The crystal structure of the Arabidopsis thaliana phototropin 1 LOV2 domain was determined in the dark-adapted state.
Here, the crystal structure of the A. thaliana phototropin 1 LOV2 domain has been determined in its dark-adapted state.
Source:
structural featuresupports
The Arabidopsis thaliana phototropin 1 LOV2 core is flanked by an N-terminal A'α helix and a C-terminal Jα helix.
The core is flanked by an N-terminal A'α helix and a C-terminal Jα helix
Source:
functional rolesupports
The LOV2 domain of phototropin 1 plays a major role in phototropism and leaf expansion.
Our results show that the LOV2 domain of phot1 plays a major role in phototropism and leaf expansion
Source:
Comparisons
Source-backed strengths
The domain has a solved dark-adapted crystal structure, providing direct structural information for the LOV2 core and its flanking A'α and Jα helices. It is reported to form a dimer through a scissor-like A'α helical interface with a short coiled coil, and the Jα helix is implicated in coiled-coil formation and dimerization. The oligomeric behavior is distinguished from Avena sativa LOV2, which was reported as monomeric.
Compared with light-oxygen-voltage sensing (LOV) domain
phototropin 1 LOV2 domain and light-oxygen-voltage sensing (LOV) domain address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: heterodimerization; same primary input modality: light
Strengths here: appears more independently replicated; looks easier to implement in practice.
Compared with optogenetic RGS2
phototropin 1 LOV2 domain and optogenetic RGS2 address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: heterodimerization; same primary input modality: light
Strengths here: appears more independently replicated; looks easier to implement in practice.
Compared with split-TurboID
phototropin 1 LOV2 domain and split-TurboID address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: heterodimerization; same primary input modality: light
Ranked Citations
- 1.
- 2.