3WKV

Voltage-gated proton channel: VSOP/Hv1 chimeric channel

Summary for 3WKV

• Entry DOI: 10.2210/pdb3wkv/pdb
• Descriptor: Ion channel (1 entity in total)
• Functional Keywords: transmembrane helix/helix/membrane protein, proton transport
• Biological source: Mus musculus (mouse)
• Total number of polymer chains: 1
• Total formula weight: 22881.96

Authors

Takeshita, K.,Sakata, S.,Yamashita, E.,Fujiwara, Y.,Kawanabe, A.,Kurokawa, T.,Okochi, Y.,Matsuda, M.,Narita, H.,Okamura, Y.,Nakagawa, A. (deposition date: 2013-10-31, release date: 2014-03-05, Last modification date: 2024-03-20)

Primary citation

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., 21:352-357, 2014

PubMed 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.

PubMed: 24584463
DOI: 10.1038/nsmb.2783

Experimental method

X-RAY DIFFRACTION (3.453 Å)