Source 1primary paper2020
Toolkit/Arabidopsis CRY2 photosensory domain
Arabidopsis CRY2 photosensory domain
Also known as: Arabidopsis CRY2, CRY2 photosensory domain
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The Arabidopsis CRY2 photosensory domain is a light-responsive protein domain from plant cryptochrome-2 whose active-state crystal structure was determined in a tetrameric form. Structural analysis indicates that this domain undergoes photo-induced oligomerization and contains specific structural elements and residues that participate in activation.
Usefulness & Problems
Why this is useful
This domain is useful as a structurally characterized light-responsive module for studying and potentially exploiting cryptochrome photoactivation. The available evidence specifically supports its value for understanding how light drives assembly of an active tetrameric state and how activation-related residues and structural elements contribute to that process.
Problem solved
It helps address the problem of defining the structural basis of plant cryptochrome activation under light. The cited study specifically resolves the photosensory domain in a tetrameric active state and identifies features implicated in photo-induced oligomerization.
Problem links
Need precise spatiotemporal control with light input
DerivedThe Arabidopsis CRY2 photosensory domain is a light-responsive protein domain from plant cryptochrome-2 whose active-state crystal structure was determined in a tetrameric form. Structural analysis indicates that this domain undergoes photo-induced oligomerization and contains specific structural elements and residues that participate in activation.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Techniques
Structural CharacterizationTarget processes
No target processes tagged yet.
Input: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: spectral hardware requirementoperating role: sensorswitch architecture: single chain
The available evidence identifies this tool specifically as the photosensory domain of Arabidopsis CRY2 and supports its use as a light-responsive protein domain. However, the provided material does not specify construct boundaries, cofactors, illumination wavelengths, expression systems, or delivery considerations.
The supplied evidence is limited to a single 2020 structural study and does not provide quantitative performance data, spectral parameters, kinetics, or application benchmarks in engineered systems. Evidence for regulation by interacting proteins is described as a proposed model rather than direct functional validation in the provided text.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Systematic structure-based analyses of photo-activated and inactive plant cryptochromes identified new structural elements and critical residues that dynamically participate in photo-induced oligomerization.
Systematic structure-based analyses of photo-activated and inactive plant CRYs elucidate new structural elements and critical residues that dynamically partake in photo-induced oligomerization.
Systematic structure-based analyses of photo-activated and inactive plant cryptochromes identified new structural elements and critical residues that dynamically participate in photo-induced oligomerization.
Systematic structure-based analyses of photo-activated and inactive plant CRYs elucidate new structural elements and critical residues that dynamically partake in photo-induced oligomerization.
Systematic structure-based analyses of photo-activated and inactive plant cryptochromes identified new structural elements and critical residues that dynamically participate in photo-induced oligomerization.
Systematic structure-based analyses of photo-activated and inactive plant CRYs elucidate new structural elements and critical residues that dynamically partake in photo-induced oligomerization.
Systematic structure-based analyses of photo-activated and inactive plant cryptochromes identified new structural elements and critical residues that dynamically participate in photo-induced oligomerization.
Systematic structure-based analyses of photo-activated and inactive plant CRYs elucidate new structural elements and critical residues that dynamically partake in photo-induced oligomerization.
Systematic structure-based analyses of photo-activated and inactive plant cryptochromes identified new structural elements and critical residues that dynamically participate in photo-induced oligomerization.
Systematic structure-based analyses of photo-activated and inactive plant CRYs elucidate new structural elements and critical residues that dynamically partake in photo-induced oligomerization.
Systematic structure-based analyses of photo-activated and inactive plant cryptochromes identified new structural elements and critical residues that dynamically participate in photo-induced oligomerization.
Systematic structure-based analyses of photo-activated and inactive plant CRYs elucidate new structural elements and critical residues that dynamically partake in photo-induced oligomerization.
The study proposes an updated model of cryptochrome photoactivation and its regulation by interacting proteins.
Our study offers an updated model of CRYs photoactivation mechanism as well as the mode of its regulation by interacting proteins.
The study proposes an updated model of cryptochrome photoactivation and its regulation by interacting proteins.
Our study offers an updated model of CRYs photoactivation mechanism as well as the mode of its regulation by interacting proteins.
The study proposes an updated model of cryptochrome photoactivation and its regulation by interacting proteins.
Our study offers an updated model of CRYs photoactivation mechanism as well as the mode of its regulation by interacting proteins.
The study proposes an updated model of cryptochrome photoactivation and its regulation by interacting proteins.
Our study offers an updated model of CRYs photoactivation mechanism as well as the mode of its regulation by interacting proteins.
The study proposes an updated model of cryptochrome photoactivation and its regulation by interacting proteins.
Our study offers an updated model of CRYs photoactivation mechanism as well as the mode of its regulation by interacting proteins.
The study proposes an updated model of cryptochrome photoactivation and its regulation by interacting proteins.
Our study offers an updated model of CRYs photoactivation mechanism as well as the mode of its regulation by interacting proteins.
The study determined the crystal structure of the photosensory domain of Arabidopsis CRY2 in a tetrameric active state.
In this study, we determine the crystal structure of the photosensory domain of Arabidopsis CRY2 in a tetrameric active state.
The study determined the crystal structure of the photosensory domain of Arabidopsis CRY2 in a tetrameric active state.
In this study, we determine the crystal structure of the photosensory domain of Arabidopsis CRY2 in a tetrameric active state.
The study determined the crystal structure of the photosensory domain of Arabidopsis CRY2 in a tetrameric active state.
In this study, we determine the crystal structure of the photosensory domain of Arabidopsis CRY2 in a tetrameric active state.
The study determined the crystal structure of the photosensory domain of Arabidopsis CRY2 in a tetrameric active state.
In this study, we determine the crystal structure of the photosensory domain of Arabidopsis CRY2 in a tetrameric active state.
The study determined the crystal structure of the photosensory domain of Arabidopsis CRY2 in a tetrameric active state.
In this study, we determine the crystal structure of the photosensory domain of Arabidopsis CRY2 in a tetrameric active state.
The study determined the crystal structure of the photosensory domain of Arabidopsis CRY2 in a tetrameric active state.
In this study, we determine the crystal structure of the photosensory domain of Arabidopsis CRY2 in a tetrameric active state.
Approval Evidence
1 source3 linked approval claimsfirst-pass slug arabidopsis-cry2-photosensory-domain
we determine the crystal structure of the photosensory domain of Arabidopsis CRY2 in a tetrameric active state
Source:
mechanistic insightsupports
Systematic structure-based analyses of photo-activated and inactive plant cryptochromes identified new structural elements and critical residues that dynamically participate in photo-induced oligomerization.
Systematic structure-based analyses of photo-activated and inactive plant CRYs elucidate new structural elements and critical residues that dynamically partake in photo-induced oligomerization.
Source:
mechanistic modelsupports
The study proposes an updated model of cryptochrome photoactivation and its regulation by interacting proteins.
Our study offers an updated model of CRYs photoactivation mechanism as well as the mode of its regulation by interacting proteins.
Source:
structural determinationsupports
The study determined the crystal structure of the photosensory domain of Arabidopsis CRY2 in a tetrameric active state.
In this study, we determine the crystal structure of the photosensory domain of Arabidopsis CRY2 in a tetrameric active state.
Source:
Comparisons
Source-backed strengths
A key strength is that the photosensory domain was structurally determined in an active tetrameric state, providing direct structural evidence for an oligomerized light-activated form. The study also reports systematic structure-based analyses that identified new structural elements and critical residues dynamically involved in photo-induced oligomerization.
Compared with CRY2 C-terminal tail
Arabidopsis CRY2 photosensory domain and CRY2 C-terminal tail address a similar problem space.
Shared frame: same top-level item type; same primary input modality: light
Arabidopsis CRY2 photosensory domain and photoactivatable inhibitor for myosin light chain kinase (MLCK) address a similar problem space.
Shared frame: same top-level item type; same primary input modality: light
Compared with PHR domain of Arabidopsis thaliana cryptochrome 2
Arabidopsis CRY2 photosensory domain and PHR domain of Arabidopsis thaliana cryptochrome 2 address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: oligomerization; same primary input modality: light
Ranked Citations
- 1.