| http://purl.uniprot.org/citations/17289589 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17289589 | http://www.w3.org/2000/01/rdf-schema#comment | "Regulatory 14-3-3 proteins activate the plant plasma membrane H(+)-ATPase by binding to its C-terminal autoinhibitory domain. This interaction requires phosphorylation of a C-terminal, mode III, recognition motif as well as an adjacent span of approximately 50 amino acids. Here we report the X-ray crystal structure of 14-3-3 in complex with the entire binding motif, revealing a previously unidentified mode of interaction. A 14-3-3 dimer simultaneously binds two H(+)-ATPase peptides, each of which forms a loop within the typical 14-3-3 binding groove and therefore exits from the center of the dimer. Several H(+)-ATPase mutants support this structure determination. Accordingly, 14-3-3 binding could result in H(+)-ATPase oligomerization. Indeed, by using single-particle electron cryomicroscopy, the 3D reconstruction of the purified H(+)-ATPase/14-3-3 complex demonstrates a hexameric arrangement. Fitting of 14-3-3 and H(+)-ATPase atomic structures into the 3D reconstruction map suggests the spatial arrangement of the holocomplex."xsd:string |
| http://purl.uniprot.org/citations/17289589 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.molcel.2006.12.017"xsd:string |
| http://purl.uniprot.org/citations/17289589 | http://purl.uniprot.org/core/author | "Boutry M."xsd:string |
| http://purl.uniprot.org/citations/17289589 | http://purl.uniprot.org/core/author | "Marco S."xsd:string |
| http://purl.uniprot.org/citations/17289589 | http://purl.uniprot.org/core/author | "Rigaud J.L."xsd:string |
| http://purl.uniprot.org/citations/17289589 | http://purl.uniprot.org/core/author | "Oecking C."xsd:string |
| http://purl.uniprot.org/citations/17289589 | http://purl.uniprot.org/core/author | "Ottmann C."xsd:string |
| http://purl.uniprot.org/citations/17289589 | http://purl.uniprot.org/core/author | "Wittinghofer A."xsd:string |
| http://purl.uniprot.org/citations/17289589 | http://purl.uniprot.org/core/author | "Weyand M."xsd:string |
| http://purl.uniprot.org/citations/17289589 | http://purl.uniprot.org/core/author | "Schauer N."xsd:string |
| http://purl.uniprot.org/citations/17289589 | http://purl.uniprot.org/core/author | "Duby G."xsd:string |
| http://purl.uniprot.org/citations/17289589 | http://purl.uniprot.org/core/author | "Marcon C."xsd:string |
| http://purl.uniprot.org/citations/17289589 | http://purl.uniprot.org/core/author | "Jaspert N."xsd:string |
| http://purl.uniprot.org/citations/17289589 | http://purl.uniprot.org/core/author | "Vandermeeren C."xsd:string |
| http://purl.uniprot.org/citations/17289589 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17289589 | http://purl.uniprot.org/core/name | "Mol Cell"xsd:string |
| http://purl.uniprot.org/citations/17289589 | http://purl.uniprot.org/core/pages | "427-440"xsd:string |
| http://purl.uniprot.org/citations/17289589 | http://purl.uniprot.org/core/title | "Structure of a 14-3-3 coordinated hexamer of the plant plasma membrane H+ -ATPase by combining X-ray crystallography and electron cryomicroscopy."xsd:string |
| http://purl.uniprot.org/citations/17289589 | http://purl.uniprot.org/core/volume | "25"xsd:string |
| http://purl.uniprot.org/citations/17289589 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17289589 |
| http://purl.uniprot.org/citations/17289589 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17289589 |
| http://purl.uniprot.org/uniprot/#_P93343-mappedCitation-17289589 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/17289589 |
| http://purl.uniprot.org/uniprot/#_Q08436-mappedCitation-17289589 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/17289589 |
| http://purl.uniprot.org/uniprot/P93343 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/17289589 |