Ontology highlight
ABSTRACT:
SUBMITTER: Symersky J
PROVIDER: S-EPMC3435195 | biostudies-literature | 2012 Aug
REPOSITORIES: biostudies-literature
Proceedings of the National Academy of Sciences of the United States of America 20120806 35
We report the high-resolution (1.9 Å) crystal structure of oligomycin bound to the subunit c(10) ring of the yeast mitochondrial ATP synthase. Oligomycin binds to the surface of the c(10) ring making contact with two neighboring molecules at a position that explains the inhibitory effect on ATP synthesis. The carboxyl side chain of Glu59, which is essential for proton translocation, forms an H-bond with oligomycin via a bridging water molecule but is otherwise shielded from the aqueous environme ...[more]