6NFQ

CopC from Pseudomonas fluorescens

Summary for 6NFQ

• Entry DOI: 10.2210/pdb6nfq/pdb
• Descriptor: CopC, COPPER (II) ION, YTTRIUM (III) ION, ... (4 entities in total)
• Functional Keywords: copc, metallochaperone, copper binding, metal binding protein
• Biological source: Pseudomonas fluorescens
• Total number of polymer chains: 3
• Total formula weight: 38204.20

Authors

Maher, M.J. (deposition date: 2018-12-20, release date: 2019-04-24, Last modification date: 2023-10-11)

Primary citation

Udagedara, S.R.,Wijekoon, C.J.K.,Xiao, Z.,Wedd, A.G.,Maher, M.J.
The crystal structure of the CopC protein from Pseudomonas fluorescens reveals amended classifications for the CopC protein family.
J. Inorg. Biochem., 195:194-200, 2019

PubMed Abstract: 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.

PubMed: 30981030
DOI: 10.1016/j.jinorgbio.2019.03.007

Experimental method

X-RAY DIFFRACTION (2 Å)