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. 2014 Apr;21(4):352-7.
doi: 10.1038/nsmb.2783. Epub 2014 Mar 2.

X-ray crystal structure of voltage-gated proton channel

Kohei Takeshita  1 , Souhei Sakata  2 , Eiki Yamashita  3 , Yuichiro Fujiwara  4 , Akira Kawanabe  4 , Tatsuki Kurokawa  5 , Yoshifumi Okochi  4 , Makoto Matsuda  3 , Hirotaka Narita  3 , Yasushi Okamura  2 , Atsushi Nakagawa  6
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X-ray crystal structure of voltage-gated proton channel

Kohei Takeshita et al. Nat Struct Mol Biol. 2014 Apr.

Abstract

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 Zn(2+). Here we present a crystal structure of mouse Hv1 in the resting state at 3.45-Å 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 Zn(2+), thus suggesting that Zn(2+) 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.

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