Ontology highlight
ABSTRACT:
SUBMITTER: Matthies D
PROVIDER: S-EPMC4228694 | biostudies-literature | 2014 Nov
REPOSITORIES: biostudies-literature
Matthies Doreen D Zhou Wenchang W Klyszejko Adriana L AL Anselmi Claudio C Yildiz Özkan Ö Brandt Karsten K Müller Volker V Faraldo-Gómez José D JD Meier Thomas T
Nature communications 20141110
All rotary ATPases catalyse the interconversion of ATP and ADP-Pi through a mechanism that is coupled to the transmembrane flow of H(+) or Na(+). Physiologically, however, F/A-type enzymes specialize in ATP synthesis driven by downhill ion diffusion, while eukaryotic V-type ATPases function as ion pumps. To begin to rationalize the molecular basis for this functional differentiation, we solved the crystal structure of the Na(+)-driven membrane rotor of the Acetobacterium woodii ATP synthase, at ...[more]