Ontology highlight
ABSTRACT:
SUBMITTER: Klusch N
PROVIDER: S-EPMC5747523 | biostudies-literature | 2017 Dec
REPOSITORIES: biostudies-literature
Klusch Niklas N Murphy Bonnie J BJ Mills Deryck J DJ Yildiz Özkan Ö Kühlbrandt Werner W
eLife 20171206
ATP synthases produce ATP by rotary catalysis, powered by the electrochemical proton gradient across the membrane. Understanding this fundamental process requires an atomic model of the proton pathway. We determined the structure of an intact mitochondrial ATP synthase dimer by electron cryo-microscopy at near-atomic resolution. Charged and polar residues of the <i>a</i>-subunit stator define two aqueous channels, each spanning one half of the membrane. Passing through a conserved membrane-intri ...[more]