2014年4月
X-ray crystal structure of voltage-gated proton channel
NATURE STRUCTURAL & MOLECULAR BIOLOGY
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- 巻
- 21
- 号
- 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
- ID情報
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- DOI : 10.1038/nsmb.2783
- ISSN : 1545-9993
- eISSN : 1545-9985
- Web of Science ID : WOS:000334349000013