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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
13
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pubmed:dateCreated |
2001-6-20
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pubmed:databankReference |
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pubmed:abstractText |
In contrast to the F-type ATPases, which use a proton gradient to generate ATP, the V-type enzymes use ATP to actively transport protons into organelles and extracellular compartments. We describe here the structure of the H-subunit (also called Vma13p) of the yeast enzyme. This is the first structure of any component of a V-type ATPase. The H-subunit is not required for assembly but plays an essential regulatory role. Despite the lack of any apparent sequence homology the structure contains five motifs similar to the so-called HEAT or armadillo repeats seen in the importins. A groove, which is occupied in the importins by the peptide that targets proteins for import into the nucleus, is occupied here by the 10 amino-terminal residues of subunit H itself. The structural similarity suggests how subunit H may interact with the ATPase itself or with other proteins. A cleft between the amino- and carboxyl-terminal domains also suggests another possible site of interaction with other factors.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-10051322,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-10201409,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-10224039,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-10340847,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-10353244,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-10485704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-10506135,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-10747882,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-10781598,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-10954728,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-1758883,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-2268628,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-5700707,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-7678431,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-7907279,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-7929308,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-8065448,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-8349704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-8377180,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-8433969,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-9144182,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-9242922,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-9442887,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-9488725,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-9620685,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11416198-9927713
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits,
http://linkedlifedata.com/resource/pubmed/chemical/Proton Pumps,
http://linkedlifedata.com/resource/pubmed/chemical/Proton-Translocating ATPases,
http://linkedlifedata.com/resource/pubmed/chemical/Vacuolar Proton-Translocating...,
http://linkedlifedata.com/resource/pubmed/chemical/unc-32 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/vha-11 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/vha-2 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/vha-3 protein, C elegans
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
98
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7134-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:11416198-Amino Acid Sequence,
pubmed-meshheading:11416198-Animals,
pubmed-meshheading:11416198-Arabidopsis,
pubmed-meshheading:11416198-Caenorhabditis elegans,
pubmed-meshheading:11416198-Caenorhabditis elegans Proteins,
pubmed-meshheading:11416198-Crystallography, X-Ray,
pubmed-meshheading:11416198-Drosophila melanogaster,
pubmed-meshheading:11416198-Humans,
pubmed-meshheading:11416198-Models, Molecular,
pubmed-meshheading:11416198-Molecular Sequence Data,
pubmed-meshheading:11416198-Protein Conformation,
pubmed-meshheading:11416198-Protein Structure, Secondary,
pubmed-meshheading:11416198-Protein Subunits,
pubmed-meshheading:11416198-Proton Pumps,
pubmed-meshheading:11416198-Proton-Translocating ATPases,
pubmed-meshheading:11416198-Saccharomyces cerevisiae,
pubmed-meshheading:11416198-Sequence Alignment,
pubmed-meshheading:11416198-Sequence Homology, Amino Acid,
pubmed-meshheading:11416198-Vacuolar Proton-Translocating ATPases
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pubmed:year |
2001
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pubmed:articleTitle |
Crystal structure of the regulatory subunit H of the V-type ATPase of Saccharomyces cerevisiae.
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pubmed:affiliation |
Institute of Molecular Biology, University of Oregon, Eugene, OR 97403-1229, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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