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Crystal structure of the red light-activated channelrhodopsin Chrimson

Author

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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
    Japan Science and Technology Agency)

  • Peter Hegemann

    (Humboldt-Universität zu Berlin)

  • Osamu Nureki

    (The University of Tokyo)

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.

Suggested Citation

  • Kazumasa Oda & Johannes Vierock & Satomi Oishi & Silvia Rodriguez-Rozada & Reiya Taniguchi & Keitaro Yamashita & J. Simon Wiegert & Tomohiro Nishizawa & Peter Hegemann & Osamu Nureki, 2018. "Crystal structure of the red light-activated channelrhodopsin Chrimson," Nature Communications, Nature, vol. 9(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-06421-9
    DOI: 10.1038/s41467-018-06421-9
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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. Amelie C. F. Bergs & Jana F. Liewald & Silvia Rodriguez-Rozada & Qiang Liu & Christin Wirt & Artur Bessel & Nadja Zeitzschel & Hilal Durmaz & Adrianna Nozownik & Holger Dill & Maëlle Jospin & Johannes, 2023. "All-optical closed-loop voltage clamp for precise control of muscles and neurons in live animals," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    3. Dennis Vettkötter & Martin Schneider & Brady D. Goulden & Holger Dill & Jana Liewald & Sandra Zeiler & Julia Guldan & Yilmaz Arda Ateş & Shigeki Watanabe & Alexander Gottschalk, 2022. "Rapid and reversible optogenetic silencing of synaptic transmission by clustering of synaptic vesicles," Nature Communications, Nature, vol. 13(1), pages 1-17, December.

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