The crystal structure of the CopC protein from Pseudomonas fluorescens reveals amended classifications for the CopC protein family
Saumya R Udagedara, Chathuri JK Wijekoon, Zhiguang Xiao, Anthony G Wedd, Megan J Maher
JOURNAL OF INORGANIC BIOCHEMISTRY | ELSEVIER SCIENCE INC | Published : 2019
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..View full abstract
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Awarded by Australian Research Council
This study was supported by the Australian Research Council grants DP140102746 to MJM and DP130100728 to AGW. Aspects of this research were undertaken on the Macromolecular Crystallography beamline MX2 at the Australian Synchrotron (Victoria, Australia) and we thank the beamline staff for their enthusiastic and professional support.