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

X-ray crystal structure of voltage-gated proton channel.

Author information

1
1] Institute for Protein Research, Osaka University, Suita, Japan. [2] Graduate School of Medicine, Osaka University, Suita, Japan. [3] Institute for Academic Initiatives, Osaka University, Suita, Japan.
2
1] Graduate School of Medicine, Osaka University, Suita, Japan. [2] Institute for Academic Initiatives, Osaka University, Suita, Japan.
3
Institute for Protein Research, Osaka University, Suita, Japan.
4
Graduate School of Medicine, Osaka University, Suita, Japan.
5
1] Graduate School of Medicine, Osaka University, Suita, Japan. [2] Present address: Graduate School of Engineering, Kyoto University, Kyoto, Japan.
6
1] Institute for Protein Research, Osaka University, Suita, Japan. [2] Institute for Academic Initiatives, Osaka University, Suita, Japan.

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.

PMID:
24584463
DOI:
10.1038/nsmb.2783
[Indexed for MEDLINE]

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