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Science 29 April 2005:
Vol. 308. no. 5722, pp. 659 - 662
DOI: 10.1126/science.1111199
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Research Articles

Structure of the Rotor Ring of F-Type Na+-ATPase from Ilyobacter tartaricus

Thomas Meier,1 Patrick Polzer,2 Kay Diederichs,2* Wolfram Welte,2 Peter Dimroth1*

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.

1 Institut für Mikrobiologie, Eidgenössische Technische Hochschule (ETH), Zürich Hönggerberg, Wolfgang-Pauli-Str. 10, CH-8093 Zürich, Switzerland.
2 Fachbereich Biologie, Universität Konstanz M656, D-78457 Konstanz, Germany.

* To whom correspondence should be addressed. E-mail: dimroth{at}micro.biol.ethz.ch (P.D.); kay.diederichs{at}uni-konstanz.de (K.D.)

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