| http://purl.uniprot.org/citations/18417453 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18417453 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18417453 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/18417453 | http://www.w3.org/2000/01/rdf-schema#comment | "As in other P-type ATPases, metal binding to transmembrane metal-binding sites (TM-MBS) in Cu(+)-ATPases is required for enzyme phosphorylation and subsequent transport. However, Cu(+) does not access Cu(+)-ATPases in a free (hydrated) form but is bound to a chaperone protein. Cu(+) transfer from Cu(+) chaperones to regulatory cytoplasmic metal-binding domains (MBDs) present in these ATPases has been described, but there is no evidence of a proposed subsequent Cu(+) movement from the MBDs to the TM-MBS. Alternatively, we postulate the parsimonious Cu(+) transfer by the chaperone directly to TM-MBS. Testing both models, the delivery of Cu(+) by Archaeoglobus fulgidus Cu(+) chaperone CopZ to the corresponding Cu(+)-ATPase, CopA, was studied. As expected, CopZ interacted with and delivered the metal to CopA MBDs. Cu(+)-loaded MBDs, acting as metal donors, were unable to activate CopA or a truncated CopA lacking MBDs. Conversely, Cu(+)-loaded CopZ activated the CopA ATPase and CopA constructs in which MBDs were rendered unable to bind Cu(+). Furthermore, under nonturnover conditions, CopZ transferred Cu(+) to the TM-MBS of a CopA lacking MBDs. These data are consistent with a model where MBDs serve a regulatory function without participating in metal transport and the chaperone delivers Cu(+) directly to transmembrane transport sites of Cu(+)-ATPases."xsd:string |
| http://purl.uniprot.org/citations/18417453 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/18417453 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/18417453 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0711446105"xsd:string |
| http://purl.uniprot.org/citations/18417453 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0711446105"xsd:string |
| http://purl.uniprot.org/citations/18417453 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18417453 |
| http://purl.uniprot.org/citations/18417453 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18417453 |
| http://purl.uniprot.org/citations/18417453 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18417453 |
| http://purl.uniprot.org/citations/18417453 | http://purl.uniprot.org/core/author | "Gonzalez-Guerrero M."xsd:string |
| http://purl.uniprot.org/citations/18417453 | http://purl.uniprot.org/core/author | "Gonzalez-Guerrero M."xsd:string |
| http://purl.uniprot.org/citations/18417453 | http://purl.uniprot.org/core/author | "Arguello J.M."xsd:string |
| http://purl.uniprot.org/citations/18417453 | http://purl.uniprot.org/core/author | "Arguello J.M."xsd:string |
| http://purl.uniprot.org/citations/18417453 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18417453 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18417453 | http://purl.uniprot.org/core/pages | "5992-5997"xsd:string |
| http://purl.uniprot.org/citations/18417453 | http://purl.uniprot.org/core/pages | "5992-5997"xsd:string |
| http://purl.uniprot.org/citations/18417453 | http://purl.uniprot.org/core/title | "Mechanism of Cu+-transporting ATPases: soluble Cu+ chaperones directly transfer Cu+ to transmembrane transport sites."xsd:string |
| http://purl.uniprot.org/citations/18417453 | http://purl.uniprot.org/core/title | "Mechanism of Cu+-transporting ATPases: soluble Cu+ chaperones directly transfer Cu+ to transmembrane transport sites."xsd:string |
| http://purl.uniprot.org/citations/18417453 | http://purl.uniprot.org/core/volume | "105"xsd:string |
| http://purl.uniprot.org/citations/18417453 | http://purl.uniprot.org/core/volume | "105"xsd:string |
| http://purl.uniprot.org/citations/18417453 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/18417453 |
| http://purl.uniprot.org/citations/18417453 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/18417453 |