Order this structure laser-etched in crystal Release date: 1996-12-07 Citations: 685 Downloads: 16354 Total score: 1581
Molecular functions: (select from list to view only structures with selected function) ATP bindingATP biosynthetic processATP catabolic processATP metabolic processATP synthesis coupled proton transportEmbryonic developmentHydrogen ion transmembrane transporter activityHydrogen ion transporting ATP synthase activity, rotational mechanismHydrogen-exporting ATPase activity, phosphorylative mechanismHydrolase activityHydrolase activity, acting on acid anhydrides, catalyzing transmembranIon transportLipid metabolic processMembraneMitochondrial inner membraneMitochondrionNegative regulation of cell adhesion involved in substrate-bound cell Nucleoside-triphosphatase activityNucleotide bindingProtein bindingProton transportProton-transporting ATP synthase complex, catalytic core F(1)Proton-transporting ATPase activity, rotational mechanismProton-transporting two-sector ATPase complexProton-transporting two-sector ATPase complex, catalytic domainTransport Scientists: (select from list to view only structures from selected author) ABRAHAMS, J.P.LESLIE, A.G.W.LUTTER, R.WALKER, J.E.				Other databases: View entry in RCSB
Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria. In the crystal structure of bovine mitochondrial F1-ATPase determined at 2.8 A resolution, the three catalytic beta-subunits differ in conformation and in the bound nucleotide. The structure supports a catalytic mechanism in intact ATP synthase in which the three catalytic subunits are in different states of the catalytic cycle at any instant. Interconversion of the states may be achieved by rotation of the alpha 3 beta 3 subassembly relative to an alpha-helical domain of the gamma-subunit. [Pubmed record]