Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 21, Issue 4, Pages 352-U170Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2783
Keywords
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Funding
- Target Proteins Research Program
- Ministry of Education, Culture, Sports, Science and Technology (MEXT) in Japan [25253016, 21229003]
- Japan Society for the Promotion of Science [24111529]
- JAXA-GCF (Japan Aerospace Exploration Agency-Granada Crystallization Facility)
- National Project on Protein Structural and Functional Analyses from the MEXT
- Academia Sinica
- National Synchrotron Radiation Research Center in Taiwan, Republic of China
- Grants-in-Aid for Scientific Research [24111529, 25860163, 26291030, 23659111, 25670108, 21229003, 25253016, 24590277, 24689012] Funding Source: KAKEN
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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.
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