Structural model of F 1 –ATPase and the implications for rotary catalysis
Open Access
- 29 April 2000
- journal article
- review article
- Published by The Royal Society in Philosophical Transactions Of The Royal Society B-Biological Sciences
- Vol. 355 (1396) , 465-471
- https://doi.org/10.1098/rstb.2000.0588
Abstract
The crystal structure of bovine mitochondrial F 1 –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 α 3 β 3 sub–assembly.Keywords
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