論文

査読有り
2014年4月

X-ray crystal structure of voltage-gated proton channel

NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • Kohei Takeshita
  • ,
  • Souhei Sakata
  • ,
  • Eiki Yamashita
  • ,
  • Yuichiro Fujiwara
  • ,
  • Akira Kawanabe
  • ,
  • Tatsuki Kurokawa
  • ,
  • Yoshifumi Okochi
  • ,
  • Makoto Matsuda
  • ,
  • Hirotaka Narita
  • ,
  • Yasushi Okamura
  • ,
  • Atsushi Nakagawa

21
4
開始ページ
352
終了ページ
U170
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1038/nsmb.2783
出版者・発行元
NATURE PUBLISHING GROUP

The voltage-gated proton channel Hv1 (or VSOP) has a voltage-sensor domain (VSD) with dual roles of voltage sensing and proton permeation. Its gating is sensitive to pH and Zn2+. Here we present a crystal structure of mouse Hv1 in the resting state at 3.45-angstrom resolution. The structure showed a 'closed umbrella' shape with a long helix consisting of the cytoplasmic coiled coil and the voltage-sensing helix, S4, and featured a wide inner-accessible vestibule. Two out of three arginines in S4 were located below the phenylalanine constituting the gating charge-transfer center. The extracellular region of each protomer coordinated a Zn2+, thus suggesting that Zn2+ stabilizes the resting state of Hv1 by competing for acidic residues that otherwise form salt bridges with voltage-sensing positive charges on S4. These findings provide a platform for understanding the general principles of voltage sensing and proton permeation.


リンク情報
DOI
https://doi.org/10.1038/nsmb.2783
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000334349000013&DestApp=WOS_CPL
ID情報
  • DOI : 10.1038/nsmb.2783
  • ISSN : 1545-9993
  • eISSN : 1545-9985
  • Web of Science ID : WOS:000334349000013

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