The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Structure of the Rotor Ring of F-Type Na + -ATPase from Ilyobacter tartaricus
Open accessAbstract
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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Self-citation
Metadata
- Authors
- Meier, T., Polzer, P., Diederichs, K., Welte, W., & Dimroth, P.
- Venue
- Science
- Published
- 2005-04-29
- Volume
- 308
- Issue
- 5722
- Pages
- 659-662
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2134593027
- Cited by
- 369
- References
- 31
- FWCI
- 13.48
- Type
- journal article
- Language
- en
- Open access
- green
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