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• W1968740095 startingPage "5992" @default.
• W1968740095 abstract "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." @default.
• W1968740095 created "2016-06-24" @default.
• W1968740095 creator A5002132250 @default.
• W1968740095 creator A5062601317 @default.
• W1968740095 date "2008-04-22" @default.
• W1968740095 modified "2023-10-14" @default.
• W1968740095 title "Mechanism of Cu ⁺ -transporting ATPases: Soluble Cu ⁺ chaperones directly transfer Cu ⁺ to transmembrane transport sites" @default.
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• W1968740095 doi "https://doi.org/10.1073/pnas.0711446105" @default.
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