Ontology highlight
ABSTRACT:
SUBMITTER: Symersky J
PROVIDER: S-EPMC3343227 | biostudies-literature | 2012 Apr
REPOSITORIES: biostudies-literature
Nature structural & molecular biology 20120415 5
The proton pore of the F(1)F(o) ATP synthase consists of a ring of c subunits, which rotates, driven by downhill proton diffusion across the membrane. An essential carboxylate side chain in each subunit provides a proton-binding site. In all the structures of c-rings reported to date, these sites are in a closed, ion-locked state. Structures are here presented of the c(10) ring from Saccharomyces cerevisiae determined at pH 8.3, 6.1 and 5.5, at resolutions of 2.0 Å, 2.5 Å and 2.0 Å, respectively ...[more]