Publication Date:
2005-04-30
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meier, Thomas -- Polzer, Patrick -- Diederichs, Kay -- Welte, Wolfram -- Dimroth, Peter -- New York, N.Y. -- Science. 2005 Apr 29;308(5722):659-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Mikrobiologie, Eidgenossische Technische Hochschule (ETH), Zurich Honggerberg, Wolfgang-Pauli-Str. 10, CH-8093 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15860619" target="_blank"〉PubMed〈/a〉
Keywords:
Adenosine Triphosphatases/*chemistry/metabolism
;
Amino Acid Sequence
;
Bacterial Proteins/*chemistry/metabolism
;
Binding Sites
;
Crystallography, X-Ray
;
Cytoplasm/metabolism
;
Fusobacteria/*enzymology
;
Glutamic Acid/chemistry/metabolism
;
Hydrophobic and Hydrophilic Interactions
;
Ion Transport
;
Models, Molecular
;
Molecular Motor Proteins/*chemistry/metabolism
;
Molecular Sequence Data
;
Protein Conformation
;
Protein Structure, Secondary
;
Protein Structure, Tertiary
;
Protein Subunits/chemistry/metabolism
;
Sodium/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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