{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Waldron KJ"],"funding":["Biotechnology and Biological Sciences Research Council"],"pagination":["32504-11"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2952252"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["285(42)"],"pubmed_abstract":["A copper-trafficking pathway was found to enable Cu(2+) occupancy of a soluble periplasm protein, CucA, even when competing Zn(2+) is abundant in the periplasm. Here, we solved the structure of CucA (a new cupin) and found that binding of Cu(2+), but not Zn(2+), quenches the fluorescence of Trp(165), which is adjacent to the metal site. Using this fluorescence probe, we established that CucA becomes partly occupied by Zn(2+) following exposure to equimolar Zn(2+) and Cu(2+). Cu(2+)-CucA is more thermodynamically stable than Zn(2+)-CucA but k((Zn→Cu)exchange) is slow, raising questions about how the periplasm contains solely the Cu(2+) form. We discovered that a copper-trafficking pathway involving two copper transporters (CtaA and PacS) and a metallochaperone (Atx1) is obligatory for Cu(2+"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Structure and metal loading of a soluble periplasm cuproprotein."],"pmcid":["PMC2952252"],"funding_grant_id":["BB/E001688/1","BBS/B/02576"],"pubmed_authors":["Robinson NJ","Waldron KJ","Firbank SJ","Tottey S","Perez-Rama M","Dainty SJ"],"additional_accession":[]},"is_claimable":false,"name":"Structure and metal loading of a soluble periplasm cuproprotein.","description":"A copper-trafficking pathway was found to enable Cu(2+) occupancy of a soluble periplasm protein, CucA, even when competing Zn(2+) is abundant in the periplasm. Here, we solved the structure of CucA (a new cupin) and found that binding of Cu(2+), but not Zn(2+), quenches the fluorescence of Trp(165), which is adjacent to the metal site. Using this fluorescence probe, we established that CucA becomes partly occupied by Zn(2+) following exposure to equimolar Zn(2+) and Cu(2+). Cu(2+)-CucA is more thermodynamically stable than Zn(2+)-CucA but k((Zn→Cu)exchange) is slow, raising questions about how the periplasm contains solely the Cu(2+) form. We discovered that a copper-trafficking pathway involving two copper transporters (CtaA and PacS) and a metallochaperone (Atx1) is obligatory for Cu(2+","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Oct","modification":"2026-04-29T18:51:56.653Z","creation":"2019-03-27T00:34:45Z"},"accession":"S-EPMC2952252","cross_references":{"pubmed":["20702411"],"doi":["10.1074/jbc.M110.153080","10.1074/jbc.m110.153080"]}}