| http://purl.uniprot.org/citations/16045926 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16045926 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
| http://purl.uniprot.org/citations/16045926 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jmb.2005.06.012"xsd:string |
| http://purl.uniprot.org/citations/16045926 | http://purl.uniprot.org/core/author | "Montgomery M.G."xsd:string |
| http://purl.uniprot.org/citations/16045926 | http://purl.uniprot.org/core/author | "Walker J.E."xsd:string |
| http://purl.uniprot.org/citations/16045926 | http://purl.uniprot.org/core/author | "Runswick M.J."xsd:string |
| http://purl.uniprot.org/citations/16045926 | http://purl.uniprot.org/core/author | "Carbajo R.J."xsd:string |
| http://purl.uniprot.org/citations/16045926 | http://purl.uniprot.org/core/author | "Neuhaus D."xsd:string |
| http://purl.uniprot.org/citations/16045926 | http://purl.uniprot.org/core/author | "Kellas F.A."xsd:string |
| http://purl.uniprot.org/citations/16045926 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/16045926 | http://purl.uniprot.org/core/name | "J Mol Biol"xsd:string |
| http://purl.uniprot.org/citations/16045926 | http://purl.uniprot.org/core/pages | "824-838"xsd:string |
| http://purl.uniprot.org/citations/16045926 | http://purl.uniprot.org/core/title | "Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit."xsd:string |
| http://purl.uniprot.org/citations/16045926 | http://purl.uniprot.org/core/volume | "351"xsd:string |
| http://purl.uniprot.org/citations/16045926 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16045926 |
| http://purl.uniprot.org/citations/16045926 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16045926 |
| http://purl.uniprot.org/uniprot/#_P13621-mappedCitation-16045926 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/16045926 |
| http://purl.uniprot.org/uniprot/P13621 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/16045926 |