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 PubMed
In 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 Also
References
- ↑ Meier T, Polzer P, Diederichs K, Welte W, Dimroth P. Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus. Science. 2005 Apr 29;308(5722):659-62. PMID:15860619 doi:308/5722/659
