1YCE

Structure of the rotor ring of F-type Na+-ATPase from Ilyobacter tartaricus

Summary for 1YCE

• Entry DOI: 10.2210/pdb1yce/pdb
• Descriptor: subunit c, SODIUM ION, NONAN-1-OL, ... (4 entities in total)
• Functional Keywords: atp synthase, na binding site, membrane protein
• Biological source: Ilyobacter tartaricus
• Total number of polymer chains: 44
• Total formula weight: 394528.11

Authors

Meier, T.,Polzer, P.,Diederichs, K.,Welte, W.,Dimroth, P. (deposition date: 2004-12-22, release date: 2005-04-12, Last modification date: 2024-02-14)

Primary citation

Meier, T.,Polzer, P.,Diederichs, K.,Welte, W.,Dimroth, P.
Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus.
Science, 308:659-662, 2005

PubMed Abstract: 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.

PubMed: 15860619
DOI: 10.1126/science.1111199

Experimental method

X-RAY DIFFRACTION (2.4 Å)