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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5722
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pubmed:dateCreated |
2005-4-29
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pubmed:databankReference |
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pubmed:abstractText |
The membrane rotor ring from the vacuolar-type (V-type) sodium ion-pumping adenosine triphosphatase (Na+-ATPase) from Enterococcus hirae consists of 10 NtpK subunits, which are homologs of the 16-kilodalton and 8-kilodalton proteolipids found in other V-ATPases and in F1Fo- or F-ATPases, respectively. Each NtpK subunit has four transmembrane alpha helices, with a sodium ion bound between helices 2 and 4 at a site buried deeply in the membrane that includes the essential residue glutamate-139. This site is probably connected to the membrane surface by two half-channels in subunit NtpI, against which the ring rotates. Symmetry mismatch between the rotor and catalytic domains appears to be an intrinsic feature of both V- and F-ATPases.
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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 |
Apr
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
29
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pubmed:volume |
308
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
654-9
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:15802565-Adenosine Triphosphatases,
pubmed-meshheading:15802565-Adenosine Triphosphate,
pubmed-meshheading:15802565-Amino Acid Sequence,
pubmed-meshheading:15802565-Bacterial Proteins,
pubmed-meshheading:15802565-Binding Sites,
pubmed-meshheading:15802565-Crystallography, X-Ray,
pubmed-meshheading:15802565-Detergents,
pubmed-meshheading:15802565-Enterococcus,
pubmed-meshheading:15802565-Ion Transport,
pubmed-meshheading:15802565-Models, Biological,
pubmed-meshheading:15802565-Models, Molecular,
pubmed-meshheading:15802565-Molecular Motor Proteins,
pubmed-meshheading:15802565-Molecular Sequence Data,
pubmed-meshheading:15802565-Phospholipids,
pubmed-meshheading:15802565-Protein Conformation,
pubmed-meshheading:15802565-Protein Structure, Tertiary,
pubmed-meshheading:15802565-Protein Subunits,
pubmed-meshheading:15802565-Sodium,
pubmed-meshheading:15802565-Static Electricity,
pubmed-meshheading:15802565-Water
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pubmed:year |
2005
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pubmed:articleTitle |
Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae.
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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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