Inhibitors of the catalytic domain of mitochondrial ATP synthase
2006 ◽
Vol 34
(5)
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pp. 989-992
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Keyword(s):
X Ray
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An understanding of the mechanism of ATP synthase requires an explanation of how inhibitors act. The catalytic F1-ATPase domain of the enzyme has been studied extensively by X-ray crystallography in a variety of inhibited states. Four independent inhibitory sites have been identified by high-resolution structural studies. They are the catalytic site, and the binding sites for the antibiotics aurovertin and efrapeptin and for the natural inhibitor protein, IF1.