Crystal structure of the channelrhodopsin light-gated cation channel

Hideaki E. Kato, Feng Zhang, Ofer Yizhar, Charu Ramakrishnan, Tomohiro Nishizawa, Kunio Hirata, Jumpei Ito, Yusuke Aita, Tomoya Tsukazaki, Shigehiko Hayashi, Peter Hegemann, Andrés D. Maturana, Ryuichiro Ishitani, Karl Deisseroth () and Osamu Nureki ()
Additional contact information
Hideaki E. Kato: Graduate School of Science, The University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan
Feng Zhang: Stanford University
Ofer Yizhar: Stanford University
Charu Ramakrishnan: Stanford University
Tomohiro Nishizawa: Graduate School of Science, The University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan
Kunio Hirata: RIKEN SPring-8 Center, Hyogo 679-5148, Japan
Jumpei Ito: Nagaoka University of Technology, Niigata 940-2188, Japan
Yusuke Aita: Nagaoka University of Technology, Niigata 940-2188, Japan
Tomoya Tsukazaki: Graduate School of Science, The University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan
Shigehiko Hayashi: Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan
Peter Hegemann: Institute of Biology, Experimental Biophysics, Humboldt-University, Invalidenstrae 42, D-10115 Berlin, Germany
Andrés D. Maturana: Nagaoka University of Technology, Niigata 940-2188, Japan
Ryuichiro Ishitani: Graduate School of Science, The University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan
Karl Deisseroth: Stanford University
Osamu Nureki: Graduate School of Science, The University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan

Nature, 2012, vol. 482, issue 7385, 369-374

Abstract: Abstract Channelrhodopsins (ChRs) are light-gated cation channels derived from algae that have shown experimental utility in optogenetics; for example, neurons expressing ChRs can be optically controlled with high temporal precision within systems as complex as freely moving mammals. Although ChRs have been broadly applied to neuroscience research, little is known about the molecular mechanisms by which these unusual and powerful proteins operate. Here we present the crystal structure of a ChR (a C1C2 chimaera between ChR1 and ChR2 from Chlamydomonas reinhardtii) at 2.3 Å resolution. The structure reveals the essential molecular architecture of ChRs, including the retinal-binding pocket and cation conduction pathway. This integration of structural and electrophysiological analyses provides insight into the molecular basis for the remarkable function of ChRs, and paves the way for the precise and principled design of ChR variants with novel properties.

Date: 2012
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DOI: 10.1038/nature10870

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