Structural model of F1-ATPase and the implications for rotary catalysis.
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.
Leslie
A G
AG
MRC Laboratory of Molecular Biology, Cambridge, UK.
Walker
J E
JE
D000818:Animals; D002417:Cattle; D018360:Crystallography, X-Ray; D046911:Macromolecular Substances; D008929:Mitochondria, Heart / Q000201:enzymology; D008958:Models, Molecular; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism*
D046911:Macromolecular Substances; D006180:Proton-Translocating ATPases