Article
Correlation between the conformational states of F1-ATPase as determined from its crystal structure and single-molecule rotation.
Proceedings of the National Academy of Sciences of the United States of America - 30 Dec 2008
Okuno Daichi, Fujisawa Ryo, Iino Ryota, Hirono-Hara Yoko, Imamura Hiromi, Noji Hiroyuki
Abstract excerpt
F(1)-ATPase is a rotary molecular motor driven by ATP hydrolysis that rotates the gamma-subunit against the alpha(3)beta(3) ring. The crystal structures of F(1), which provide the structural basis for the catalysis mechanism, have shown essentially 1 stable conformational state. In contrast, single-molecule studies have revealed that F(1) has 2 stable conformational states: ATP-binding dwell state and catalytic...
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