|Title||Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus.|
|Publication Type||Journal Article|
|Year of Publication||2005|
|Authors||Meier, T, Polzer, P, Diederichs, K, Welte, W, Dimroth, P|
|Date Published||2005 Apr 29|
|Keywords||Adenosine Triphosphatases, Amino Acid Sequence, Bacterial Proteins, Binding Sites, Crystallography, X-Ray, Cytoplasm, Fusobacteria, Glutamic Acid, Hydrophobic and Hydrophilic Interactions, Ion Transport, Models, Molecular, Molecular Motor Proteins, Molecular Sequence Data, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Subunits, Sodium|
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.