Journal
NATURE COMMUNICATIONS
Volume 9, Issue -, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41467-018-06421-9
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Funding
- MEXT [16H06294]
- JSPS KAKENHI [17J06203, 17H05000]
- Deutsche Forschungsgemeinschaft DFG [SFB1078, SPP 1926]
- Deutsche Forschungsgemeinschaft DFG [Cluster of Excellence Unifying Concepts in Catalysis, UniCat, BIG-NSE]
- Deutsche Forschungsgemeinschaft DFG [E4]
- EU-Project STARDUST
- European Research Council [ERC-2016-StG 714762]
- JST, PRESTO [JPMJPR14L8]
- Grants-in-Aid for Scientific Research [17J06203, 17H05000] Funding Source: KAKEN
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Channelrhodopsins are light-activated ion channels that mediate cation permeation across cell membranes upon light absorption. Red-light-activated channelrhodopsins are of particular interest, because red light penetrates deeper into biological tissues and also enables dual-color experiments in combination with blue-light-activated optogenetic tools. Here we report the crystal structure of the most red-shifted channelrhodopsin from the algae Chlamydomonas noctigama, Chrimson, at 2.6 angstrom resolution. Chrimson resembles prokaryotic proton pumps in the retinal binding pocket, while sharing similarity with other channelrhodopsins in the ion-conducting pore. Concomitant mutation analysis identified the structural features that are responsible for Chrimson's red light sensitivity; namely, the protonation of the counterion for the retinal Schiff base, and the polar residue distribution and rigidity of the retinal binding pocket. Based on these mechanistic insights, we engineered ChrimsonSA, a mutant with a maximum activation wavelength red-shifted beyond 605 nm and accelerated closing kinetics.
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