Science manuscript MS 1111199 Supporting online material Structure of the rotor ring of F-type Na + -ATPase from Ilyobacter tartaricus
Source (2005)
- ISSN: 10959203
- DOI: 10.1126/science.1111199
- PubMed: 15860619
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Abstract
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.
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