Inhibitors of the catalytic domain of mitochondrial ATP synthase.

TitleInhibitors of the catalytic domain of mitochondrial ATP synthase.
Publication TypeJournal Article
Year of Publication2006
AuthorsGledhill, JR, Walker, JE
JournalBiochem Soc Trans
Volume34
IssuePt 5
Pagination989-92
Date Published2006 Nov
ISSN0300-5127
KeywordsCatalytic Domain, Dicyclohexylcarbodiimide, Enzyme Inhibitors, Mitochondrial Proton-Translocating ATPases, Models, Molecular, Protein Conformation
Abstract

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.

DOI10.1042/BST0340989
Alternate JournalBiochem. Soc. Trans.
Citation Key10.1042/BST0340989
PubMed ID17052243
Grant ListMC_U105663150 / / Medical Research Council / United Kingdom