期刊
PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY OF LONDON SERIES B-BIOLOGICAL SCIENCES
卷 355, 期 1396, 页码 465-471出版社
ROYAL SOC LONDON
DOI: 10.1098/rstb.2000.0588
关键词
F-1-ATPase; crystal structure; rotary catalysis
类别
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 gamma-subunit relative to the approximately spherical alpha(3)beta(3) sub-assembly.
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