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Crystal structure of the red light-activated channelrhodopsin Chrimson

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Crystal structure of the red light-activated channelrhodopsin Chrimson. / Oda, Kazumasa; Vierock, Johannes; Oishi, Satomi; Rodriguez-Rozada, Silvia; Taniguchi, Reiya; Yamashita, Keitaro; Wiegert, J Simon; Nishizawa, Tomohiro; Hegemann, Peter; Nureki, Osamu.

in: NAT COMMUN, Jahrgang 9, Nr. 1, 26.09.2018, S. 3949.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Oda, K, Vierock, J, Oishi, S, Rodriguez-Rozada, S, Taniguchi, R, Yamashita, K, Wiegert, JS, Nishizawa, T, Hegemann, P & Nureki, O 2018, 'Crystal structure of the red light-activated channelrhodopsin Chrimson', NAT COMMUN, Jg. 9, Nr. 1, S. 3949. https://doi.org/10.1038/s41467-018-06421-9

APA

Oda, K., Vierock, J., Oishi, S., Rodriguez-Rozada, S., Taniguchi, R., Yamashita, K., Wiegert, J. S., Nishizawa, T., Hegemann, P., & Nureki, O. (2018). Crystal structure of the red light-activated channelrhodopsin Chrimson. NAT COMMUN, 9(1), 3949. https://doi.org/10.1038/s41467-018-06421-9

Vancouver

Oda K, Vierock J, Oishi S, Rodriguez-Rozada S, Taniguchi R, Yamashita K et al. Crystal structure of the red light-activated channelrhodopsin Chrimson. NAT COMMUN. 2018 Sep 26;9(1):3949. https://doi.org/10.1038/s41467-018-06421-9

Bibtex

@article{c65b49a89680451c9294b36976215059,
title = "Crystal structure of the red light-activated channelrhodopsin Chrimson",
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 {\AA} 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.",
keywords = "Journal Article",
author = "Kazumasa Oda and Johannes Vierock and Satomi Oishi and Silvia Rodriguez-Rozada and Reiya Taniguchi and Keitaro Yamashita and Wiegert, {J Simon} and Tomohiro Nishizawa and Peter Hegemann and Osamu Nureki",
year = "2018",
month = sep,
day = "26",
doi = "10.1038/s41467-018-06421-9",
language = "English",
volume = "9",
pages = "3949",
journal = "NAT COMMUN",
issn = "2041-1723",
publisher = "NATURE PUBLISHING GROUP",
number = "1",

}

RIS

TY - JOUR

T1 - Crystal structure of the red light-activated channelrhodopsin Chrimson

AU - Oda, Kazumasa

AU - Vierock, Johannes

AU - Oishi, Satomi

AU - Rodriguez-Rozada, Silvia

AU - Taniguchi, Reiya

AU - Yamashita, Keitaro

AU - Wiegert, J Simon

AU - Nishizawa, Tomohiro

AU - Hegemann, Peter

AU - Nureki, Osamu

PY - 2018/9/26

Y1 - 2018/9/26

N2 - 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.

AB - 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.

KW - Journal Article

U2 - 10.1038/s41467-018-06421-9

DO - 10.1038/s41467-018-06421-9

M3 - SCORING: Journal article

C2 - 30258177

VL - 9

SP - 3949

JO - NAT COMMUN

JF - NAT COMMUN

SN - 2041-1723

IS - 1

ER -