The crystal structure of the CopC protein from Pseudomonas fluorescens reveals amended classifications for the CopC protein family
| Autor: | Saumya R. Udagedara, Chathuri J.K. Wijekoon, Zhiguang Xiao, Anthony G. Wedd, Megan J. Maher |
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| Rok vydání: | 2018 |
| Předmět: |
0303 health sciences
Binding Sites Protein Conformation 030302 biochemistry & molecular biology Crystallography X-Ray Ligands Pseudomonas fluorescens Biochemistry Inorganic Chemistry 03 medical and health sciences Bacterial Proteins Mutation Amino Acid Sequence Sequence Alignment Copper 030304 developmental biology Protein Binding |
| Zdroj: | Journal of inorganic biochemistry. 195 |
| ISSN: | 1873-3344 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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