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

Thomas Meier | Zendy; Patrick Polzer | Zendy; Kay Diederichs | Zendy; Wolfram Welte | Zendy; Peter Dimroth | Zendy

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

Author(s) -

Thomas Meier,

Patrick Polzer,

Kay Diederichs,

Wolfram Welte,

Peter Dimroth

Publication year - 2005

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.1111199

Subject(s) - atp synthase , chemistry , crystallography , atpase , protein subunit , adenosine triphosphate , ion , ring (chemistry) , biophysics , membrane , angstrom , rotor (electric) , stereochemistry , enzyme , physics , biology , biochemistry , organic chemistry , gene , quantum mechanics

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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