Structural highlights
Publication Abstract from PubMed
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-A 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.
X-ray crystal structure of voltage-gated proton channel.,Takeshita K, Sakata S, Yamashita E, Fujiwara Y, Kawanabe A, Kurokawa T, Okochi Y, Matsuda M, Narita H, Okamura Y, Nakagawa A Nat Struct Mol Biol. 2014 Apr;21(4):352-7. doi: 10.1038/nsmb.2783. Epub 2014 Mar , 2. PMID:24584463[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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References
- ↑ Takeshita K, Sakata S, Yamashita E, Fujiwara Y, Kawanabe A, Kurokawa T, Okochi Y, Matsuda M, Narita H, Okamura Y, Nakagawa A. X-ray crystal structure of voltage-gated proton channel. Nat Struct Mol Biol. 2014 Apr;21(4):352-7. doi: 10.1038/nsmb.2783. Epub 2014 Mar , 2. PMID:24584463 doi:http://dx.doi.org/10.1038/nsmb.2783
