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Article

The 3.5-Å CryoEM Structure of Nanodisc-Reconstituted Yeast Vacuolar ATPase Vo Proton Channel.

Molecular cell - 15 Mar 2018

Roh Soung-Hun, Stam Nicholas J, Hryc Corey F, Couoh-Cardel Sergio, Pintilie Grigore, Chiu Wah, Wilkens Stephan

Abstract excerpt

The molecular mechanism of transmembrane proton translocation in rotary motor ATPases is not fully understood. Here, we report the 3.5-Å resolution cryoEM structure of the lipid nanodisc-reconstituted Vo proton channel of the yeast vacuolar H+-ATPase, captured in a physiologically relevant, autoinhibited state. The resulting atomic model provides structural detail for the amino acids that constitute the proton...

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Identifiers

PMID: 29526695
DOI: 10.1016/j.molcel.2018.02.006
PMCID: PMC5893162

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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