Publikation: Structure of the Rotor Ring of F-Type NA+-ATPase from Ilyobacter tartaricus
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2005
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Science. 2005, 308(5722), pp. 659-662. ISSN 0036-8075. eISSN 1095-9203
Zusammenfassung
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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570 Biowissenschaften, Biologie
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MEIER, Thomas, Patrick POLZER, Kay DIEDERICHS, Wolfram WELTE, Peter DIMROTH, 2005. Structure of the Rotor Ring of F-Type NA+-ATPase from Ilyobacter tartaricus. In: Science. 2005, 308(5722), pp. 659-662. ISSN 0036-8075. eISSN 1095-9203BibTex
@article{Meier2005Struc-6683,
year={2005},
title={Structure of the Rotor Ring of F-Type NA+-ATPase from Ilyobacter tartaricus},
number={5722},
volume={308},
issn={0036-8075},
journal={Science},
pages={659--662},
author={Meier, Thomas and Polzer, Patrick and Diederichs, Kay and Welte, Wolfram and Dimroth, Peter}
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<dcterms:abstract xml:lang="eng">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.</dcterms:abstract>
<dc:contributor>Dimroth, Peter</dc:contributor>
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<dc:contributor>Polzer, Patrick</dc:contributor>
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