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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5445
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pubmed:dateCreated |
1999-12-14
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pubmed:databankReference |
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pubmed:abstractText |
Adenosine triphosphate (ATP) synthase contains a rotary motor involved in biological energy conversion. Its membrane-embedded F0 sector has a rotation generator fueled by the proton-motive force, which provides the energy required for the synthesis of ATP by the F1 domain. An electron density map obtained from crystals of a subcomplex of yeast mitochondrial ATP synthase shows a ring of 10 c subunits. Each c subunit forms an alpha-helical hairpin. The interhelical loops of six to seven of the c subunits are in close contact with the gamma and delta subunits of the central stalk. The extensive contact between the c ring and the stalk suggests that they may rotate as an ensemble during catalysis.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
286
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1700-5
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pubmed:dateRevised |
2007-3-19
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pubmed:meshHeading |
pubmed-meshheading:10576729-Adenosine Triphosphate,
pubmed-meshheading:10576729-Catalysis,
pubmed-meshheading:10576729-Crystallization,
pubmed-meshheading:10576729-Crystallography, X-Ray,
pubmed-meshheading:10576729-Hydrogen Bonding,
pubmed-meshheading:10576729-Mitochondria,
pubmed-meshheading:10576729-Models, Molecular,
pubmed-meshheading:10576729-Molecular Motor Proteins,
pubmed-meshheading:10576729-Protein Conformation,
pubmed-meshheading:10576729-Protein Folding,
pubmed-meshheading:10576729-Protein Structure, Secondary,
pubmed-meshheading:10576729-Proton-Motive Force,
pubmed-meshheading:10576729-Proton-Translocating ATPases,
pubmed-meshheading:10576729-Protons,
pubmed-meshheading:10576729-Saccharomyces cerevisiae
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pubmed:year |
1999
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pubmed:articleTitle |
Molecular architecture of the rotary motor in ATP synthase.
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pubmed:affiliation |
Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge CB2 2XY, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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