title: Inhibitors of the catalytic domain of mitochondrial ATP synthase.
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.
authors.affiliation: MRC Dunn Human Nutrition Unit, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 2XY, UK.
authors.forename: J R
authors.initials: JR
authors.lastname: Gledhill
authors.forename: J E
authors.initials: JE
authors.lastname: Walker
mesh_terms: D020134:Catalytic Domain; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D025261:Mitochondrial Proton-Translocating ATPases / Q000037:antagonists & inhibitors* / Q000737:chemistry; D008958:Models, Molecular; D011487:Protein Conformation
chemical_list: D004791:Enzyme Inhibitors; D004024:Dicyclohexylcarbodiimide; D025261:Mitochondrial Proton-Translocating ATPases