Journal article

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

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..

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