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

TitleStructure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus.
Publication TypeJournal Article
Year of Publication2005
AuthorsMeier, T, Polzer, P, Diederichs, K, Welte, W, Dimroth, P
JournalScience
Volume308
Issue5722
Pagination659-62
Date Published2005 Apr 29
ISSN1095-9203
KeywordsAdenosine 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
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.

DOI10.1126/science.1111199
Alternate JournalScience
Citation Key10.1126/science.1111199
PubMed ID15860619