Source 1primary paper2014Proceedings of the National Academy of Sciences
Toolkit/EL346
EL346
Also known as: blue light-activated HK from Erythrobacter litoralis HTCC2594
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
EL346 is a full-length blue light-activated histidine kinase from Erythrobacter litoralis HTCC2594 that contains a LOV photosensor domain. Structural evidence indicates that the LOV domain regulates kinase state by controlling intramolecular domain interactions, maintaining an inhibited dark-state conformation, and releasing that inhibition upon photoactivation.
Usefulness & Problems
Why this is useful
EL346 is useful as a mechanistically defined model for blue-light regulation of histidine kinase signaling. It provides a structurally characterized example of how a LOV sensor domain can couple light input to kinase control through intramolecular inhibition and dimerization-related regulation.
Problem solved
EL346 helps address the problem of understanding how sensory light input is transduced into histidine kinase output at the level of full-length domain architecture. The reported structure specifically clarifies how dark-state inhibition and light-dependent changes in domain interfaces can regulate kinase activity.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
dark-state autoinhibitiondimerization controlHeterodimerizationlight-dependent allosteric switchinglight-induced weakening of interdomain interactionsTechniques
No technique tags yet.
Target processes
signalingInput: Light
Implementation Constraints
EL346 is a full-length protein from Erythrobacter litoralis HTCC2594 and includes a LOV sensor domain linked to histidine kinase output regions including DHpL and CA domains. The available evidence supports blue-light responsiveness, but the supplied material does not provide construct design details, cofactor requirements, expression conditions, or delivery guidance.
The evidence provided is limited to a single structural study and associated mechanistic interpretation. The supplied record does not describe independent replication, quantitative activity measurements, spectral parameters, or validation across multiple biological contexts.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
The DHpL domain contacts the CA domain and keeps EL346 in an inhibited conformation in the dark.
The DHpL domain also contacts the catalytic/ATP-binding (CA) domain, keeping EL346 in an inhibited conformation in the dark.
The DHpL domain contacts the CA domain and keeps EL346 in an inhibited conformation in the dark.
The DHpL domain also contacts the catalytic/ATP-binding (CA) domain, keeping EL346 in an inhibited conformation in the dark.
The DHpL domain contacts the CA domain and keeps EL346 in an inhibited conformation in the dark.
The DHpL domain also contacts the catalytic/ATP-binding (CA) domain, keeping EL346 in an inhibited conformation in the dark.
The DHpL domain contacts the CA domain and keeps EL346 in an inhibited conformation in the dark.
The DHpL domain also contacts the catalytic/ATP-binding (CA) domain, keeping EL346 in an inhibited conformation in the dark.
The DHpL domain contacts the CA domain and keeps EL346 in an inhibited conformation in the dark.
The DHpL domain also contacts the catalytic/ATP-binding (CA) domain, keeping EL346 in an inhibited conformation in the dark.
The DHpL domain contacts the CA domain and keeps EL346 in an inhibited conformation in the dark.
The DHpL domain also contacts the catalytic/ATP-binding (CA) domain, keeping EL346 in an inhibited conformation in the dark.
The DHpL domain contacts the CA domain and keeps EL346 in an inhibited conformation in the dark.
The DHpL domain also contacts the catalytic/ATP-binding (CA) domain, keeping EL346 in an inhibited conformation in the dark.
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
Light stimulation weakens interdomain interactions to facilitate EL346 activation.
Upon light stimulation, interdomain interactions weaken to facilitate activation.
Light stimulation weakens interdomain interactions to facilitate EL346 activation.
Upon light stimulation, interdomain interactions weaken to facilitate activation.
Light stimulation weakens interdomain interactions to facilitate EL346 activation.
Upon light stimulation, interdomain interactions weaken to facilitate activation.
Light stimulation weakens interdomain interactions to facilitate EL346 activation.
Upon light stimulation, interdomain interactions weaken to facilitate activation.
Light stimulation weakens interdomain interactions to facilitate EL346 activation.
Upon light stimulation, interdomain interactions weaken to facilitate activation.
Light stimulation weakens interdomain interactions to facilitate EL346 activation.
Upon light stimulation, interdomain interactions weaken to facilitate activation.
Light stimulation weakens interdomain interactions to facilitate EL346 activation.
Upon light stimulation, interdomain interactions weaken to facilitate activation.
EL346 functions as a monomer rather than as a dimeric histidine kinase.
Contrary to the standard view that signaling occurs within HK dimers, EL346 functions as a monomer.
EL346 functions as a monomer rather than as a dimeric histidine kinase.
Contrary to the standard view that signaling occurs within HK dimers, EL346 functions as a monomer.
EL346 functions as a monomer rather than as a dimeric histidine kinase.
Contrary to the standard view that signaling occurs within HK dimers, EL346 functions as a monomer.
EL346 functions as a monomer rather than as a dimeric histidine kinase.
Contrary to the standard view that signaling occurs within HK dimers, EL346 functions as a monomer.
EL346 functions as a monomer rather than as a dimeric histidine kinase.
Contrary to the standard view that signaling occurs within HK dimers, EL346 functions as a monomer.
EL346 functions as a monomer rather than as a dimeric histidine kinase.
Contrary to the standard view that signaling occurs within HK dimers, EL346 functions as a monomer.
EL346 functions as a monomer rather than as a dimeric histidine kinase.
Contrary to the standard view that signaling occurs within HK dimers, EL346 functions as a monomer.
Approval Evidence
1 source5 linked approval claimsfirst-pass slug el346
Here, we report the full-length structure of a blue light-activated HK from Erythrobacter litoralis HTCC2594 (EL346)
Source:
dark state inhibitionsupports
The DHpL domain contacts the CA domain and keeps EL346 in an inhibited conformation in the dark.
The DHpL domain also contacts the catalytic/ATP-binding (CA) domain, keeping EL346 in an inhibited conformation in the dark.
Source:
mechanism of regulationsupports
The LOV sensor domain controls kinase activity and prevents dimerization by binding one side of the DHpL domain.
Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain.
Source:
mechanistic modelsupports
The LOV domain controls kinase activity by affecting stability of the DHpL/CA interface and releasing the CA domain from an inhibited conformation upon photoactivation.
Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation.
Source:
photoactivation mechanismsupports
Light stimulation weakens interdomain interactions to facilitate EL346 activation.
Upon light stimulation, interdomain interactions weaken to facilitate activation.
Source:
structural statesupports
EL346 functions as a monomer rather than as a dimeric histidine kinase.
Contrary to the standard view that signaling occurs within HK dimers, EL346 functions as a monomer.
Source:
Comparisons
Source-backed strengths
A key strength is the availability of full-length structural evidence for the intact blue light-activated histidine kinase. The cited study supports a specific mechanistic model in which the LOV domain binds one side of the DHpL domain, affects the DHpL/CA interface, prevents dimerization, and relieves CA-domain inhibition upon photoactivation.
Ranked Citations
- 1.