| pubmed-article:16045926 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16045926 | lifeskim:mentions | umls-concept:C0007452 | lld:lifeskim |
| pubmed-article:16045926 | lifeskim:mentions | umls-concept:C1412669 | lld:lifeskim |
| pubmed-article:16045926 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:16045926 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:16045926 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:16045926 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:16045926 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:16045926 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:16045926 | lifeskim:mentions | umls-concept:C1063749 | lld:lifeskim |
| pubmed-article:16045926 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:16045926 | pubmed:dateCreated | 2005-8-8 | lld:pubmed |
| pubmed-article:16045926 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16045926 | pubmed:abstractText | The peripheral stalk of ATP synthase holds the alpha3beta3 catalytic subcomplex stationary against the torque of the rotating central stalk. In bovine mitochondria, the N-terminal domain of the oligomycin sensitivity conferral protein (OSCP-NT; residues 1-120) anchors one end of the peripheral stalk to the N-terminal tails of one or more alpha-subunits of the F1 subcomplex. Here we present the solution structure of OSCP-NT and an NMR titration study of its interaction with peptides representing N-terminal tails of F1 alpha-subunits. The structure comprises a bundle of six alpha-helices, and its interaction site contains adjoining hydrophobic surfaces of helices 1 and 5; residues in the region 1-8 of the alpha-subunit are essential for the interaction. The OSCP-NT is similar to the N-terminal domain of the delta-subunit from Escherichia coli ATP synthase (delta-NT), except that their surface charges differ (basic and acidic, respectively). As the charges of the adjacent crown regions in their alpha3beta3 complexes are similar, the OSCP-NT and delta-NT probably do not contact the crowns extensively. The N-terminal tails of alpha-subunit tails are probably alpha-helical, and so this interface, which is essential for the rotary mechanism of the enzyme, appears to consist of helix-helix interactions. | lld:pubmed |
| pubmed-article:16045926 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16045926 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16045926 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16045926 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16045926 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16045926 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16045926 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16045926 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16045926 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16045926 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16045926 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16045926 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16045926 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:16045926 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:16045926 | pubmed:author | pubmed-author:NeuhausDavidD | lld:pubmed |
| pubmed-article:16045926 | pubmed:author | pubmed-author:WalkerJohn... | lld:pubmed |
| pubmed-article:16045926 | pubmed:author | pubmed-author:RunswickMicha... | lld:pubmed |
| pubmed-article:16045926 | pubmed:author | pubmed-author:CarbajoRodrig... | lld:pubmed |
| pubmed-article:16045926 | pubmed:author | pubmed-author:MontgomeryMar... | lld:pubmed |
| pubmed-article:16045926 | pubmed:author | pubmed-author:KellasFiona... | lld:pubmed |
| pubmed-article:16045926 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16045926 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:16045926 | pubmed:volume | 351 | lld:pubmed |
| pubmed-article:16045926 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16045926 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16045926 | pubmed:pagination | 824-38 | lld:pubmed |
| pubmed-article:16045926 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:16045926 | pubmed:meshHeading | pubmed-meshheading:16045926... | lld:pubmed |
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| pubmed-article:16045926 | pubmed:meshHeading | pubmed-meshheading:16045926... | lld:pubmed |
| pubmed-article:16045926 | pubmed:meshHeading | pubmed-meshheading:16045926... | lld:pubmed |
| pubmed-article:16045926 | pubmed:meshHeading | pubmed-meshheading:16045926... | lld:pubmed |
| pubmed-article:16045926 | pubmed:meshHeading | pubmed-meshheading:16045926... | lld:pubmed |
| pubmed-article:16045926 | pubmed:meshHeading | pubmed-meshheading:16045926... | lld:pubmed |
| pubmed-article:16045926 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16045926 | pubmed:articleTitle | Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit. | lld:pubmed |
| pubmed-article:16045926 | pubmed:affiliation | MRC Dunn Human Nutrition Unit, Hills Road, Cambridge CB2 2XY, UK. | lld:pubmed |
| pubmed-article:16045926 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16045926 | pubmed:publicationType | In Vitro | lld:pubmed |
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