Structural model of F1-ATPase and the implications for rotary catalysis.

TitleStructural model of F1-ATPase and the implications for rotary catalysis.
Publication TypeJournal Article
Year of Publication2000
AuthorsLeslie, AG, Walker, JE
JournalPhilos Trans R Soc Lond B Biol Sci
Volume355
Issue1396
Pagination465-71
Date Published2000 Apr 29
ISSN0962-8436
KeywordsAnimals, Cattle, Crystallography, X-Ray, Macromolecular Substances, Mitochondria, Heart, Models, Molecular, Protein Conformation, Proton-Translocating ATPases
Abstract

The crystal structure of bovine mitochondrial F1-ATPase is described. Several features of the structure are consistent with the binding change mechanism of catalysis, in which binding of substrates induces conformational changes that result in a high degree of cooperativity between the three catalytic sites. Furthermore, the structure also suggests that catalysis is accompanied by a physical rotation of the centrally placed gamma-subunit relative to the approximately spherical alpha3beta3 subassembly.

DOI10.1098/rstb.2000.0588
Alternate JournalPhilos. Trans. R. Soc. Lond., B, Biol. Sci.
Citation Key10.1098/rstb.2000.0588
PubMed ID10836500
PubMed Central IDPMC1692760