Your browser version may not work well with NCBI's Web applications. More information here...
1: Science. 2005 Apr 29;308(5722):659-62.
Related Articles, Links
Click here to read Click here to read
Comment in:
Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus.

Meier T, Polzer P, Diederichs K, Welte W, Dimroth P.

Institut für Mikrobiologie, Eidgenössische Technische Hochschule (ETH), Zürich Hönggerberg, Wolfgang-Pauli-Str. 10, CH-8093 Zürich, Switzerland.

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.

Publication Types:
PMID: 15860619 [PubMed - indexed for MEDLINE]