Ontology highlight
ABSTRACT:
SUBMITTER: Roh SH
PROVIDER: S-EPMC5893162 | biostudies-literature | 2018 Mar
REPOSITORIES: biostudies-literature
Roh Soung-Hun SH Stam Nicholas J NJ Hryc Corey F CF Couoh-Cardel Sergio S Pintilie Grigore G Chiu Wah W Wilkens Stephan S
Molecular cell 20180308 6
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 V<sub>o</sub> proton channel of the yeast vacuolar H<sup>+</sup>-ATPase, captured in a physiologically relevant, autoinhibited state. The resulting atomic model provides structural detail for the amino acids that constitute the proton pathway at the interface of the proteolipid ring and subunit a. ...[more]