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Crystal structure of the channelrhodopsin light-gated cation channel

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Listed:
  • 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)

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.

Suggested Citation

  • 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. Matur, 2012. "Crystal structure of the channelrhodopsin light-gated cation channel," Nature, Nature, vol. 482(7385), pages 369-374, February.
    • Handle: RePEc:nat:nature:v:482:y:2012:i:7385:d:10.1038_nature10870
    DOI: 10.1038/nature10870
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    Cited by:

    1. Kyle Tucker & Savitha Sridharan & Hillel Adesnik & Stephen G. Brohawn, 2022. "Cryo-EM structures of the channelrhodopsin ChRmine in lipid nanodiscs," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    2. Claire N Bedbrook & Kevin K Yang & Austin J Rice & Viviana Gradinaru & Frances H Arnold, 2017. "Machine learning to design integral membrane channelrhodopsins for efficient eukaryotic expression and plasma membrane localization," PLOS Computational Biology, Public Library of Science, vol. 13(10), pages 1-21, October.
    3. Takefumi Morizumi & Kyumhyuk Kim & Hai Li & Elena G. Govorunova & Oleg A. Sineshchekov & Yumei Wang & Lei Zheng & Éva Bertalan & Ana-Nicoleta Bondar & Azam Askari & Leonid S. Brown & John L. Spudich &, 2023. "Structures of channelrhodopsin paralogs in peptidiscs explain their contrasting K+ and Na+ selectivities," Nature Communications, Nature, vol. 14(1), pages 1-13, December.

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