Source 1primary paper2025PPR
Toolkit/ChR024
ChR024
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
ChR024 is a red-shifted cation-conducting channelrhodopsin that functions as a light-gated ion channel. Structural and electrophysiological analyses place it within a pump-fold channelrhodopsin architecture while supporting passive cation conductance and color tuning.
Usefulness & Problems
Why this is useful
ChR024 is useful as a red-shifted optogenetic actuator candidate because it combines light-gated channel activity with a channelrhodopsin scaffold related to outward proton pumps. The available evidence indicates value for studying how pump-fold rhodopsins can support passive ion conductance and for expanding the diversity of light-responsive ion channels.
Source:
ChR024 is a cation-conducting channelrhodopsin with a red-shifted absorption spectrum
Problem solved
ChR024 helps address the problem of identifying and characterizing red-shifted channelrhodopsins from previously unrecognized sequence space. It also provides an example relevant to the mechanistic problem of how an outward proton pump fold can be converted into a light-gated channel.
Problem links
provides a red-shifted pump-fold channelrhodopsin model for studying color tuning and passive ion conductance
LiteratureIt provides a structurally characterized red-shifted channelrhodopsin relevant to rational engineering of next-generation optogenetic tools. It also helps define the boundary between pump-type and channel-type rhodopsins.
Source:
It provides a structurally characterized red-shifted channelrhodopsin relevant to rational engineering of next-generation optogenetic tools. It also helps define the boundary between pump-type and channel-type rhodopsins.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A reusable architecture pattern for arranging parts into an engineered system.
Techniques
Structural CharacterizationTarget processes
No target processes tagged yet.
Input: Light
Implementation Constraints
cofactor dependency: requires exogenous cofactorencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: spectral hardware requirementoperating role: actuator
ChR024 is a light-input rhodopsin construct analyzed by structural characterization and electrophysiology. The provided evidence does not specify construct design, retinal/cofactor requirements, expression system, trafficking features, or illumination parameters.
The supplied evidence does not report quantitative performance metrics such as action spectrum peak, photocurrent amplitude, kinetics, ion selectivity ratios, or expression behavior. Independent replication and validation across organisms, cell types, or in vivo settings are not described in the provided material.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
ChR024 was discovered through machine-learning–guided gene mining from a previously unidentified clade.
recently discovered from a previously unidentified clade through machine-learning–guided gene mining
ChR024 was discovered through machine-learning–guided gene mining from a previously unidentified clade.
recently discovered from a previously unidentified clade through machine-learning–guided gene mining
ChR024 was discovered through machine-learning–guided gene mining from a previously unidentified clade.
recently discovered from a previously unidentified clade through machine-learning–guided gene mining
ChR024 was discovered through machine-learning–guided gene mining from a previously unidentified clade.
recently discovered from a previously unidentified clade through machine-learning–guided gene mining
ChR024 was discovered through machine-learning–guided gene mining from a previously unidentified clade.
recently discovered from a previously unidentified clade through machine-learning–guided gene mining
ChR024 was discovered through machine-learning–guided gene mining from a previously unidentified clade.
recently discovered from a previously unidentified clade through machine-learning–guided gene mining
ChR024 was discovered through machine-learning–guided gene mining from a previously unidentified clade.
recently discovered from a previously unidentified clade through machine-learning–guided gene mining
ChR024 was discovered through machine-learning–guided gene mining from a previously unidentified clade.
recently discovered from a previously unidentified clade through machine-learning–guided gene mining
Comparative structural analysis combined with electrophysiology demonstrates conversion of an outward proton pump into a light-gated channel.
comparative structural analysis of channel- and pump-type rhodopsins, combined with electrophysiology, provides insights into the molecular boundary between these two functional classes and demonstrates the conversion of an outward proton pump into a light-gated channel
Comparative structural analysis combined with electrophysiology demonstrates conversion of an outward proton pump into a light-gated channel.
comparative structural analysis of channel- and pump-type rhodopsins, combined with electrophysiology, provides insights into the molecular boundary between these two functional classes and demonstrates the conversion of an outward proton pump into a light-gated channel
Comparative structural analysis combined with electrophysiology demonstrates conversion of an outward proton pump into a light-gated channel.
comparative structural analysis of channel- and pump-type rhodopsins, combined with electrophysiology, provides insights into the molecular boundary between these two functional classes and demonstrates the conversion of an outward proton pump into a light-gated channel
Comparative structural analysis combined with electrophysiology demonstrates conversion of an outward proton pump into a light-gated channel.
comparative structural analysis of channel- and pump-type rhodopsins, combined with electrophysiology, provides insights into the molecular boundary between these two functional classes and demonstrates the conversion of an outward proton pump into a light-gated channel
Comparative structural analysis combined with electrophysiology demonstrates conversion of an outward proton pump into a light-gated channel.
comparative structural analysis of channel- and pump-type rhodopsins, combined with electrophysiology, provides insights into the molecular boundary between these two functional classes and demonstrates the conversion of an outward proton pump into a light-gated channel
Comparative structural analysis combined with electrophysiology demonstrates conversion of an outward proton pump into a light-gated channel.
comparative structural analysis of channel- and pump-type rhodopsins, combined with electrophysiology, provides insights into the molecular boundary between these two functional classes and demonstrates the conversion of an outward proton pump into a light-gated channel
Comparative structural analysis combined with electrophysiology demonstrates conversion of an outward proton pump into a light-gated channel.
comparative structural analysis of channel- and pump-type rhodopsins, combined with electrophysiology, provides insights into the molecular boundary between these two functional classes and demonstrates the conversion of an outward proton pump into a light-gated channel
Comparative structural analysis combined with electrophysiology demonstrates conversion of an outward proton pump into a light-gated channel.
comparative structural analysis of channel- and pump-type rhodopsins, combined with electrophysiology, provides insights into the molecular boundary between these two functional classes and demonstrates the conversion of an outward proton pump into a light-gated channel
ChR024 is a red-shifted cation-conducting channelrhodopsin.
ChR024 is a cation-conducting channelrhodopsin with a red-shifted absorption spectrum
ChR024 is a red-shifted cation-conducting channelrhodopsin.
ChR024 is a cation-conducting channelrhodopsin with a red-shifted absorption spectrum
ChR024 is a red-shifted cation-conducting channelrhodopsin.
ChR024 is a cation-conducting channelrhodopsin with a red-shifted absorption spectrum
ChR024 is a red-shifted cation-conducting channelrhodopsin.
ChR024 is a cation-conducting channelrhodopsin with a red-shifted absorption spectrum
ChR024 is a red-shifted cation-conducting channelrhodopsin.
ChR024 is a cation-conducting channelrhodopsin with a red-shifted absorption spectrum
ChR024 is a red-shifted cation-conducting channelrhodopsin.
ChR024 is a cation-conducting channelrhodopsin with a red-shifted absorption spectrum
ChR024 is a red-shifted cation-conducting channelrhodopsin.
ChR024 is a cation-conducting channelrhodopsin with a red-shifted absorption spectrum
ChR024 is a red-shifted cation-conducting channelrhodopsin.
ChR024 is a cation-conducting channelrhodopsin with a red-shifted absorption spectrum
Charged residues close to and distant from the retinal chromophore cooperatively modulate the pKa of the Schiff base counterion and thereby determine the absorption maximum wavelength in ChR024.
charged residues close and distant from the retinal chromophore cooperatively modulate the pKa of the Schiff base counterion and thereby determine the absorption maximum wavelength
Charged residues close to and distant from the retinal chromophore cooperatively modulate the pKa of the Schiff base counterion and thereby determine the absorption maximum wavelength in ChR024.
charged residues close and distant from the retinal chromophore cooperatively modulate the pKa of the Schiff base counterion and thereby determine the absorption maximum wavelength
Charged residues close to and distant from the retinal chromophore cooperatively modulate the pKa of the Schiff base counterion and thereby determine the absorption maximum wavelength in ChR024.
charged residues close and distant from the retinal chromophore cooperatively modulate the pKa of the Schiff base counterion and thereby determine the absorption maximum wavelength
Charged residues close to and distant from the retinal chromophore cooperatively modulate the pKa of the Schiff base counterion and thereby determine the absorption maximum wavelength in ChR024.
charged residues close and distant from the retinal chromophore cooperatively modulate the pKa of the Schiff base counterion and thereby determine the absorption maximum wavelength
Charged residues close to and distant from the retinal chromophore cooperatively modulate the pKa of the Schiff base counterion and thereby determine the absorption maximum wavelength in ChR024.
charged residues close and distant from the retinal chromophore cooperatively modulate the pKa of the Schiff base counterion and thereby determine the absorption maximum wavelength
Charged residues close to and distant from the retinal chromophore cooperatively modulate the pKa of the Schiff base counterion and thereby determine the absorption maximum wavelength in ChR024.
charged residues close and distant from the retinal chromophore cooperatively modulate the pKa of the Schiff base counterion and thereby determine the absorption maximum wavelength
Charged residues close to and distant from the retinal chromophore cooperatively modulate the pKa of the Schiff base counterion and thereby determine the absorption maximum wavelength in ChR024.
charged residues close and distant from the retinal chromophore cooperatively modulate the pKa of the Schiff base counterion and thereby determine the absorption maximum wavelength
Charged residues close to and distant from the retinal chromophore cooperatively modulate the pKa of the Schiff base counterion and thereby determine the absorption maximum wavelength in ChR024.
charged residues close and distant from the retinal chromophore cooperatively modulate the pKa of the Schiff base counterion and thereby determine the absorption maximum wavelength
ChR024 has an architecture strikingly similar to ion-pumping rhodopsins, even more so than ChRmine.
The structures reveal an architecture strikingly similar to that of ion-pumping rhodopsins, even more so than other pump-like channelrhodopsins such as ChRmine.
ChR024 has an architecture strikingly similar to ion-pumping rhodopsins, even more so than ChRmine.
The structures reveal an architecture strikingly similar to that of ion-pumping rhodopsins, even more so than other pump-like channelrhodopsins such as ChRmine.
ChR024 has an architecture strikingly similar to ion-pumping rhodopsins, even more so than ChRmine.
The structures reveal an architecture strikingly similar to that of ion-pumping rhodopsins, even more so than other pump-like channelrhodopsins such as ChRmine.
ChR024 has an architecture strikingly similar to ion-pumping rhodopsins, even more so than ChRmine.
The structures reveal an architecture strikingly similar to that of ion-pumping rhodopsins, even more so than other pump-like channelrhodopsins such as ChRmine.
ChR024 has an architecture strikingly similar to ion-pumping rhodopsins, even more so than ChRmine.
The structures reveal an architecture strikingly similar to that of ion-pumping rhodopsins, even more so than other pump-like channelrhodopsins such as ChRmine.
ChR024 has an architecture strikingly similar to ion-pumping rhodopsins, even more so than ChRmine.
The structures reveal an architecture strikingly similar to that of ion-pumping rhodopsins, even more so than other pump-like channelrhodopsins such as ChRmine.
ChR024 has an architecture strikingly similar to ion-pumping rhodopsins, even more so than ChRmine.
The structures reveal an architecture strikingly similar to that of ion-pumping rhodopsins, even more so than other pump-like channelrhodopsins such as ChRmine.
ChR024 has an architecture strikingly similar to ion-pumping rhodopsins, even more so than ChRmine.
The structures reveal an architecture strikingly similar to that of ion-pumping rhodopsins, even more so than other pump-like channelrhodopsins such as ChRmine.
Cryo-EM structures of ChR024 were determined in detergent micelles and lipid nanodiscs at 3.22 Å and 2.45 Å resolution, respectively.
we present cryo-electron microscopy structures of ChR024 in detergent micelles and lipid nanodiscs at resolutions of 3.22 and 2.45 Å, respectively
cryo-EM resolution in detergent micelles 3.22 Åcryo-EM resolution in lipid nanodiscs 2.45 Å
Cryo-EM structures of ChR024 were determined in detergent micelles and lipid nanodiscs at 3.22 Å and 2.45 Å resolution, respectively.
we present cryo-electron microscopy structures of ChR024 in detergent micelles and lipid nanodiscs at resolutions of 3.22 and 2.45 Å, respectively
cryo-EM resolution in detergent micelles 3.22 Åcryo-EM resolution in lipid nanodiscs 2.45 Å
Cryo-EM structures of ChR024 were determined in detergent micelles and lipid nanodiscs at 3.22 Å and 2.45 Å resolution, respectively.
we present cryo-electron microscopy structures of ChR024 in detergent micelles and lipid nanodiscs at resolutions of 3.22 and 2.45 Å, respectively
cryo-EM resolution in detergent micelles 3.22 Åcryo-EM resolution in lipid nanodiscs 2.45 Å
Cryo-EM structures of ChR024 were determined in detergent micelles and lipid nanodiscs at 3.22 Å and 2.45 Å resolution, respectively.
we present cryo-electron microscopy structures of ChR024 in detergent micelles and lipid nanodiscs at resolutions of 3.22 and 2.45 Å, respectively
cryo-EM resolution in detergent micelles 3.22 Åcryo-EM resolution in lipid nanodiscs 2.45 Å
Cryo-EM structures of ChR024 were determined in detergent micelles and lipid nanodiscs at 3.22 Å and 2.45 Å resolution, respectively.
we present cryo-electron microscopy structures of ChR024 in detergent micelles and lipid nanodiscs at resolutions of 3.22 and 2.45 Å, respectively
cryo-EM resolution in detergent micelles 3.22 Åcryo-EM resolution in lipid nanodiscs 2.45 Å
Cryo-EM structures of ChR024 were determined in detergent micelles and lipid nanodiscs at 3.22 Å and 2.45 Å resolution, respectively.
we present cryo-electron microscopy structures of ChR024 in detergent micelles and lipid nanodiscs at resolutions of 3.22 and 2.45 Å, respectively
cryo-EM resolution in detergent micelles 3.22 Åcryo-EM resolution in lipid nanodiscs 2.45 Å
Cryo-EM structures of ChR024 were determined in detergent micelles and lipid nanodiscs at 3.22 Å and 2.45 Å resolution, respectively.
we present cryo-electron microscopy structures of ChR024 in detergent micelles and lipid nanodiscs at resolutions of 3.22 and 2.45 Å, respectively
cryo-EM resolution in detergent micelles 3.22 Åcryo-EM resolution in lipid nanodiscs 2.45 Å
Cryo-EM structures of ChR024 were determined in detergent micelles and lipid nanodiscs at 3.22 Å and 2.45 Å resolution, respectively.
we present cryo-electron microscopy structures of ChR024 in detergent micelles and lipid nanodiscs at resolutions of 3.22 and 2.45 Å, respectively
cryo-EM resolution in detergent micelles 3.22 Åcryo-EM resolution in lipid nanodiscs 2.45 Å
Approval Evidence
1 source6 linked approval claimsfirst-pass slug chr024
ChR024 is a cation-conducting channelrhodopsin with a red-shifted absorption spectrum.
Source:
discovery methodsupports
ChR024 was discovered through machine-learning–guided gene mining from a previously unidentified clade.
recently discovered from a previously unidentified clade through machine-learning–guided gene mining
Source:
engineering resultsupports
Comparative structural analysis combined with electrophysiology demonstrates conversion of an outward proton pump into a light-gated channel.
comparative structural analysis of channel- and pump-type rhodopsins, combined with electrophysiology, provides insights into the molecular boundary between these two functional classes and demonstrates the conversion of an outward proton pump into a light-gated channel
Source:
functional propertysupports
ChR024 is a red-shifted cation-conducting channelrhodopsin.
ChR024 is a cation-conducting channelrhodopsin with a red-shifted absorption spectrum
Source:
mechanismsupports
Charged residues close to and distant from the retinal chromophore cooperatively modulate the pKa of the Schiff base counterion and thereby determine the absorption maximum wavelength in ChR024.
charged residues close and distant from the retinal chromophore cooperatively modulate the pKa of the Schiff base counterion and thereby determine the absorption maximum wavelength
Source:
structural comparisonsupports
ChR024 has an architecture strikingly similar to ion-pumping rhodopsins, even more so than ChRmine.
The structures reveal an architecture strikingly similar to that of ion-pumping rhodopsins, even more so than other pump-like channelrhodopsins such as ChRmine.
Source:
structural resultsupports
Cryo-EM structures of ChR024 were determined in detergent micelles and lipid nanodiscs at 3.22 Å and 2.45 Å resolution, respectively.
we present cryo-electron microscopy structures of ChR024 in detergent micelles and lipid nanodiscs at resolutions of 3.22 and 2.45 Å, respectively
Source:
Comparisons
Source-stated alternatives
The abstract explicitly contrasts ChR024 with ChRmine as another pump-like channelrhodopsin. The web research summary also identifies C1C2, Chrimson, KnChR, GtCCR2, KCR1, and Coccomyxa rhodopsin as nearby comparators.
Source:
The abstract explicitly contrasts ChR024 with ChRmine as another pump-like channelrhodopsin. The web research summary also identifies C1C2, Chrimson, KnChR, GtCCR2, KCR1, and Coccomyxa rhodopsin as nearby comparators.
Source-backed strengths
The reported strengths are its red-shifted spectral property, passive cation conductance, and support from both structural analysis and electrophysiology. Its discovery from a previously unidentified clade by machine-learning-guided gene mining also suggests that it expands the known diversity of channelrhodopsins.
Source:
comparative structural analysis of channel- and pump-type rhodopsins, combined with electrophysiology, provides insights into the molecular boundary between these two functional classes and demonstrates the conversion of an outward proton pump into a light-gated channel
Compared with KnChR
The abstract explicitly contrasts ChR024 with ChRmine as another pump-like channelrhodopsin. The web research summary also identifies C1C2, Chrimson, KnChR, GtCCR2, KCR1, and Coccomyxa rhodopsin as nearby comparators.
Shared frame: source-stated alternative in extracted literature
Strengths here: red-shifted absorption spectrum; cation-conducting channelrhodopsin; architecture is strongly similar to ion-pumping rhodopsins.
Relative tradeoffs: structure and function were previously poorly understood.
Source:
The abstract explicitly contrasts ChR024 with ChRmine as another pump-like channelrhodopsin. The web research summary also identifies C1C2, Chrimson, KnChR, GtCCR2, KCR1, and Coccomyxa rhodopsin as nearby comparators.
Ranked Citations
- 1.