Structural basis for Na+ transport mechanism by a light-driven Na+ pump

Hideaki E. Kato, Keiichi Inoue, Rei Abe-Yoshizumi, Yoshitaka Kato, Hikaru Ono, Masae Konno, Shoko Hososhima, Toru Ishizuka, Mohammad Razuanul Hoque, Hirofumi Kunitomo, Jumpei Ito, Susumu Yoshizawa, Keitaro Yamashita, Mizuki Takemoto, Tomohiro Nishizawa, Reiya Taniguchi, Kazuhiro Kogure, Andrés D. Maturana, Yuichi Iino, Hiromu Yawo, Ryuichiro Ishitani, Hideki Kandori () and Osamu Nureki ()
Additional contact information
Hideaki E. Kato: Graduate School of Science, The University of Tokyo
Keiichi Inoue: Nagoya Institute of Technology
Rei Abe-Yoshizumi: Nagoya Institute of Technology
Yoshitaka Kato: Nagoya Institute of Technology
Hikaru Ono: Nagoya Institute of Technology
Masae Konno: Nagoya Institute of Technology
Shoko Hososhima: Tohoku University Graduate School of Life Sciences
Toru Ishizuka: Tohoku University Graduate School of Life Sciences
Mohammad Razuanul Hoque: Tohoku University Graduate School of Life Sciences
Hirofumi Kunitomo: Graduate School of Science, The University of Tokyo
Jumpei Ito: Graduate School of Bioagricultural Sciences, Nagoya University
Susumu Yoshizawa: Atmosphere and Ocean Research Institute, The University of Tokyo
Keitaro Yamashita: RIKEN SPring-8 Center
Mizuki Takemoto: Graduate School of Science, The University of Tokyo
Tomohiro Nishizawa: Graduate School of Science, The University of Tokyo
Reiya Taniguchi: Graduate School of Science, The University of Tokyo
Kazuhiro Kogure: Atmosphere and Ocean Research Institute, The University of Tokyo
Andrés D. Maturana: Graduate School of Bioagricultural Sciences, Nagoya University
Yuichi Iino: Graduate School of Science, The University of Tokyo
Hiromu Yawo: Tohoku University Graduate School of Life Sciences
Ryuichiro Ishitani: Graduate School of Science, The University of Tokyo
Hideki Kandori: Nagoya Institute of Technology
Osamu Nureki: Graduate School of Science, The University of Tokyo

Nature, 2015, vol. 521, issue 7550, 48-53

Abstract: Abstract Krokinobacter eikastus rhodopsin 2 (KR2) is the first light-driven Na+ pump discovered, and is viewed as a potential next-generation optogenetics tool. Since the positively charged Schiff base proton, located within the ion-conducting pathway of all light-driven ion pumps, was thought to prohibit the transport of a non-proton cation, the discovery of KR2 raised the question of how it achieves Na+ transport. Here we present crystal structures of KR2 under neutral and acidic conditions, which represent the resting and M-like intermediate states, respectively. Structural and spectroscopic analyses revealed the gating mechanism, whereby the flipping of Asp116 sequesters the Schiff base proton from the conducting pathway to facilitate Na+ transport. Together with the structure-based engineering of the first light-driven K+ pumps, electrophysiological assays in mammalian neurons and behavioural assays in a nematode, our studies reveal the molecular basis for light-driven non-proton cation pumps and thus provide a framework that may advance the development of next-generation optogenetics.

Date: 2015
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DOI: 10.1038/nature14322

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