Crystal structure of the red light-activated channelrhodopsin Chrimson

Channelrhodopsins are light-activated ion channels that mediate cation permeation across cell membranes upon light absorption. Here, the authors report the crystal structure of the most red-shifted channelrhodopsin from the algae Chlamydomonas noctigama at 2.6 Å resolution.

Bibliographic Details
Main Authors:	Kazumasa Oda, Johannes Vierock, Satomi Oishi, Silvia Rodriguez-Rozada, Reiya Taniguchi, Keitaro Yamashita, J. Simon Wiegert, Tomohiro Nishizawa, Peter Hegemann, Osamu Nureki
Format:	Article
Language:	English
Published:	Nature Publishing Group 2018-09-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-018-06421-9

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spelling	doaj-2e2e42256ee040838fd207078c313d722021-05-11T09:47:17ZengNature Publishing GroupNature Communications2041-17232018-09-019111110.1038/s41467-018-06421-9Crystal structure of the red light-activated channelrhodopsin ChrimsonKazumasa Oda0Johannes Vierock1Satomi Oishi2Silvia Rodriguez-Rozada3Reiya Taniguchi4Keitaro Yamashita5J. Simon Wiegert6Tomohiro Nishizawa7Peter Hegemann8Osamu Nureki9Department of Biological Sciences Graduate School of Science, The University of TokyoInstitute of Biology, Experimental Biophysics, Humboldt-Universität zu BerlinDepartment of Biological Sciences Graduate School of Science, The University of TokyoResearch Group Synaptic Wiring and Information Processing, Center for Molecular Neurobiology Hamburg (ZMNH)Department of Biological Sciences Graduate School of Science, The University of TokyoRIKEN SPring-8 CenterResearch Group Synaptic Wiring and Information Processing, Center for Molecular Neurobiology Hamburg (ZMNH)Department of Biological Sciences Graduate School of Science, The University of TokyoInstitute of Biology, Experimental Biophysics, Humboldt-Universität zu BerlinDepartment of Biological Sciences Graduate School of Science, The University of TokyoChannelrhodopsins are light-activated ion channels that mediate cation permeation across cell membranes upon light absorption. Here, the authors report the crystal structure of the most red-shifted channelrhodopsin from the algae Chlamydomonas noctigama at 2.6 Å resolution.https://doi.org/10.1038/s41467-018-06421-9
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Kazumasa Oda Johannes Vierock Satomi Oishi Silvia Rodriguez-Rozada Reiya Taniguchi Keitaro Yamashita J. Simon Wiegert Tomohiro Nishizawa Peter Hegemann Osamu Nureki
spellingShingle	Kazumasa Oda Johannes Vierock Satomi Oishi Silvia Rodriguez-Rozada Reiya Taniguchi Keitaro Yamashita J. Simon Wiegert Tomohiro Nishizawa Peter Hegemann Osamu Nureki Crystal structure of the red light-activated channelrhodopsin Chrimson Nature Communications
author_facet	Kazumasa Oda Johannes Vierock Satomi Oishi Silvia Rodriguez-Rozada Reiya Taniguchi Keitaro Yamashita J. Simon Wiegert Tomohiro Nishizawa Peter Hegemann Osamu Nureki
author_sort	Kazumasa Oda
title	Crystal structure of the red light-activated channelrhodopsin Chrimson
title_short	Crystal structure of the red light-activated channelrhodopsin Chrimson
title_full	Crystal structure of the red light-activated channelrhodopsin Chrimson
title_fullStr	Crystal structure of the red light-activated channelrhodopsin Chrimson
title_full_unstemmed	Crystal structure of the red light-activated channelrhodopsin Chrimson
title_sort	crystal structure of the red light-activated channelrhodopsin chrimson
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2018-09-01
description	Channelrhodopsins are light-activated ion channels that mediate cation permeation across cell membranes upon light absorption. Here, the authors report the crystal structure of the most red-shifted channelrhodopsin from the algae Chlamydomonas noctigama at 2.6 Å resolution.
url	https://doi.org/10.1038/s41467-018-06421-9
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Crystal structure of the red light-activated channelrhodopsin Chrimson

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