Crystal structure of the red light-activated channelrhodopsin Chrimson

Kazumasa Oda, Johannes Vierock, Satomi Oishi, Silvia Rodriguez-Rozada, Reiya Taniguchi, Keitaro Yamashita, J. Simon Wiegert, Tomohiro Nishizawa (), Peter Hegemann () and Osamu Nureki ()
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Kazumasa Oda: The University of Tokyo
Johannes Vierock: Humboldt-Universität zu Berlin
Satomi Oishi: The University of Tokyo
Silvia Rodriguez-Rozada: Center for Molecular Neurobiology Hamburg (ZMNH)
Reiya Taniguchi: The University of Tokyo
Keitaro Yamashita: RIKEN SPring-8 Center
J. Simon Wiegert: Center for Molecular Neurobiology Hamburg (ZMNH)
Tomohiro Nishizawa: The University of Tokyo
Peter Hegemann: Humboldt-Universität zu Berlin
Osamu Nureki: The University of Tokyo

Nature Communications, 2018, vol. 9, issue 1, 1-11

Abstract: Abstract 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 Å 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.

Date: 2018
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DOI: 10.1038/s41467-018-06421-9

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