Structural model of F-1-ATPase and the implications for rotary catalysis

The crystal structure of bovine mitochondrial F-1-ATPase is described. Seve ral features of the structure are consistent with the binding change mechan ism of catalysis, in which binding of substrates induces conformational cha nges that result in a high degree of cooperativity between the three cataly tic sites. Furthermore, the structure also suggests that catalysis is accom panied by a physical rotation of the centrally placed gamma-subunit relativ e to the approximately spherical alpha(3)beta(3) sub-assembly.