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

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2005
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Meier, Thomas
Polzer, Patrick
Dimroth, Peter
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Science ; 308 (2005), 5722. - S. 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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ISO 690MEIER, 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. 308(5722), pp. 659-662. ISSN 0036-8075. eISSN 1095-9203
BibTex
@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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