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

被引：59

作者：

Leslie, AGW

Walker, JE

机构：

[1] MRC, Mol Biol Lab, Cambridge CB2 2QH, England

[2] MRC, Dunn Human Nutr Unit, Cambridge CB2 2XY, England

来源：

PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY OF LONDON SERIES B-BIOLOGICAL SCIENCES | 2000年 / 355卷 / 1396期

关键词：

F-1-ATPase; crystal structure; rotary catalysis;

D O I：

10.1098/rstb.2000.0588

中图分类号：

Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

收藏

页码：465 / 471

页数：7

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