A structure-based model for the synthesis and hydrolysis of ATP by F1-ATPase

被引：131
作者：
Gao, YQ
Yang, W
Karplus, M [1 ]
机构：
[1] Harvard Univ, Dept Chem & Chem Biol, Cambridge, MA 02138 USA
[2] Univ Strasbourg 1, Lab Chim Biophys, ISIS, F-67000 Strasbourg, France
来源：
CELL | 2005年 / 123卷 / 02期
关键词：
D O I：
10.1016/j.cell.2005.10.001
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Many essential functions of living cells are performed by nanoscale protein motors. The best characterized of these is F0F1-ATP synthase, the smallest rotary motor. This rotary motor catalyzes the synthesis of ATP with high efficiency under conditions where the reactants (ADP, H2PO4-) and the product (ATP) are present in the cell at similar concentrations. We present a detailed structure-based kinetic model for the mechanism of action of F-1-ATPase and demonstrate the role of different protein conformations for substrate binding during ATP synthesis and ATP hydrolysis. The model shows that the pathway for ATP hydrolysis is not simply the pathway for ATP synthesis in reverse. The findings of the model also explain why the cellular concentration of ATP does not inhibit ATP synthesis.
引用
收藏
页码：195 / 205
页数：11
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