1yce | pdb_00001yce
From Proteopedia
Structure of the rotor ring of F-type Na+-ATPase from Ilyobacter tartaricus
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Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn the crystal structure of the membrane-embedded rotor ring of the sodium ion-translocating adenosine 5'-triphosphate (ATP) synthase of Ilyobacter tartaricus at 2.4 angstrom resolution, 11 c subunits are assembled into an hourglass-shaped cylinder with 11-fold symmetry. Sodium ions are bound in a locked conformation close to the outer surface of the cylinder near the middle of the membrane. The structure supports an ion-translocation mechanism in the intact ATP synthase in which the binding site converts from the locked conformation into one that opens toward subunit a as the rotor ring moves through the subunit a/c interface. Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus.,Meier T, Polzer P, Diederichs K, Welte W, Dimroth P Science. 2005 Apr 29;308(5722):659-62. PMID:15860619[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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This page was last modified 12:29, 10 September 2015.