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Crystal structure of the natural anion-conducting channelrhodopsin GtACR1
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Crystal structure of the natural anion-conducting channelrhodopsin GtACR1
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Journal Article
Crystal structure of the natural anion-conducting channelrhodopsin GtACR1
2018
Overview
The naturally occurring channelrhodopsin variant anion channelrhodopsin-1 (ACR1), discovered in the cryptophyte algae
Guillardia theta
, exhibits large light-gated anion conductance and high anion selectivity when expressed in heterologous settings, properties that support its use as an optogenetic tool to inhibit neuronal firing with light. However, molecular insight into ACR1 is lacking owing to the absence of structural information underlying light-gated anion conductance. Here we present the crystal structure of
G. theta
ACR1 at 2.9 Å resolution. The structure reveals unusual architectural features that span the extracellular domain, retinal-binding pocket, Schiff-base region, and anion-conduction pathway. Together with electrophysiological and spectroscopic analyses, these findings reveal the fundamental molecular basis of naturally occurring light-gated anion conductance, and provide a framework for designing the next generation of optogenetic tools.
The crystal structure of anion channelrhodopsin-1 (ACR1) from the algae
Guillardia theta
provides insights into the basis of anion conductance.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 82
/ 82/83
/ Algae
/ Anions
/ Bacteriorhodopsins - chemistry
/ Channelrhodopsins - chemistry
/ Channelrhodopsins - metabolism
/ Channelrhodopsins - radiation effects
/ Humanities and Social Sciences
/ Ion Channel Gating - radiation effects
/ Ion Transport - radiation effects
/ Light
/ Neurons
/ Proteins
/ Retina
/ Science
