Royal Society Publishing

Structural model of F1–ATPase and the implications for rotary catalysis

A. G. W. Leslie, J. E. Walker

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 γ–subunit relative to the approximately spherical α3β3 sub–assembly.

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