Work

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

Year: 2005

Type: article

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.

Source: Science

DOI: 10.1126/science.1111199

Authors: Thomas Meier, Patrick Polzer, Kay Diederichs, Wolfram Welte, Peter Dimroth

Institutions: University of Konstanz, ETH Zurich, Institute of Microbiology

Language: English

Topic: ATP Synthase and ATPases Research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

OpenAlex ID: W2134593027

FWCI: 11.92

Cites: 34

Cited by: 371

Related to: 10