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The crystal structure of the CopC protein from Pseudomonas fluorescens reveals amended classifications for the CopC protein family.

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.

journal_name

J Inorg Biochem

journal_title

Journal of inorganic biochemistry

authors

Udagedara SR,Wijekoon CJK,Xiao Z,Wedd AG,Maher MJ

doi

10.1016/j.jinorgbio.2019.03.007

subject

Has Abstract

pub_date

2019-06-01 00:00:00

pages

194-200

eissn

0162-0134

issn

1873-3344

pii

S0162-0134(18)30753-0

journal_volume

195

pub_type

杂志文章

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