6nfr | pdb_00006nfr

CopC from Pseudomonas fluorescens

spinqualitylabelsall models 6nfr, resolution 1.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6nfr is a 1 chain structure with sequence from "bacillus_fluorescens_liquefaciens"_flugge_1886 "bacillus fluorescens liquefaciens" flugge 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The bacterial CopC family of proteins are periplasmic copper binding proteins that act in copper detoxification. These proteins contain Cu(I) and/or Cu(II) binding sites, with the family that binds Cu(II) only the most prevalent, based on sequence analyses. Here we present three crystal structures of the CopC protein from Pseudomonas fluorescens (Pf-CopC) that include the wild type protein bound to Cu(II) and two variant proteins, where Cu(II) coordinating ligands were mutated, in Cu-free states. We show that the Cu(II) atom in Pf-CopC is coordinated by two His residues, an Asp residue and the N-terminus of the protein (therefore a 3N+O site). This coordination structure is consistent with all structurally characterized proteins from the CopC family to date. Structural and sequence analyses of the CopC family allow a relationship between protein sequence and the Cu(II) binding affinity of these proteins to be proposed. The crystal structure of the CopC protein from Pseudomonas fluorescens reveals amended classifications for the CopC protein family.,Udagedara SR, Wijekoon CJK, Xiao Z, Wedd AG, Maher MJ J Inorg Biochem. 2019 Mar 21;195:194-200. doi: 10.1016/j.jinorgbio.2019.03.007. PMID:30981030 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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