Journal
ELIFE
Volume 10, Issue -, Pages -Publisher
eLIFE SCIENCES PUBL LTD
DOI: 10.7554/eLife.62389
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Funding
- Japan Society for the Promotion of Science [16H06294, 18J21256, 17H05000]
- Japan Science and Technology Agency [JPMJPR14L9, JPMJPR14L8]
- Japan Agency for Medical Research and Development
- Deutsche Forschungsgemeinschaft [SFB1078 (B2)]
- Cluster of Excellence in Inflammation Research
- Cluster of Excellence in Inflammation Research [SPP 1926]
- European Research Council [ERC-2016-StG 714762]
- Hertie Foundation
- Ministry of Education, Culture, Sports, Science and Technology
- Grants-in-Aid for Scientific Research [17H05000, 18J21256] Funding Source: KAKEN
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Channelrhodopsins (ChRs) are microbial light-gated ion channels used in optogenetics for controlling neural activity with light. Time-resolved crystallographic analyses revealed conformational changes in ChR following photoactivation, suggesting early changes in the pore-forming helices trigger the opening of the ion conducting pore.
Channelrhodopsins (ChRs) are microbial light-gated ion channels utilized in optogenetics to control neural activity with light. Light absorption causes retinal chromophore isomerization and subsequent protein conformational changes visualized as optically distinguished intermediates, coupled with channel opening and closing. However, the detailed molecular events underlying channel gating remain unknown. We performed time-resolved serial femtosecond crystallographic analyses of ChR by using an X-ray free electron laser, which revealed conformational changes following photoactivation. The isomerized retinal adopts a twisted conformation and shifts toward the putative internal proton donor residues, consequently inducing an outward shift of TM3, as well as a local deformation in TM7. These early conformational changes in the pore-forming helices should be the triggers that lead to opening of the ion conducting pore.
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