5ICU
The crystal structure of CopC from Methylosinus trichosporium OB3b
Summary for 5ICU
| Entry DOI | 10.2210/pdb5icu/pdb |
| Descriptor | CopC, COPPER (II) ION, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | copc, metal homeostasis, pcoc, chaperone, cupredoxin |
| Biological source | Methylosinus trichosporium OB3b |
| Total number of polymer chains | 1 |
| Total formula weight | 11209.49 |
| Authors | Lawton, T.J.,Hurley, J.D.,Rosenzweig, A.C. (deposition date: 2016-02-23, release date: 2016-04-06, Last modification date: 2024-03-06) |
| Primary citation | Lawton, T.J.,Kenney, G.E.,Hurley, J.D.,Rosenzweig, A.C. The CopC Family: Structural and Bioinformatic Insights into a Diverse Group of Periplasmic Copper Binding Proteins. Biochemistry, 55:2278-2290, 2016 Cited by PubMed Abstract: The CopC proteins are periplasmic copper binding proteins believed to play a role in bacterial copper homeostasis. Previous studies have focused on CopCs that are part of seven-protein Cop or Pco systems involved in copper resistance. These canonical CopCs contain distinct Cu(I) and Cu(II) binding sites. Mounting evidence suggests that CopCs are more widely distributed, often present only with the CopD inner membrane protein, frequently as a fusion protein, and that the CopC and CopD proteins together function in the uptake of copper to the cytoplasm. In the methanotroph Methylosinus trichosporium OB3b, genes encoding a CopCD pair are located adjacent to the particulate methane monooxygenase (pMMO) operon. The CopC from this organism (Mst-CopC) was expressed, purified, and structurally characterized. The 1.46 Å resolution crystal structure of Mst-CopC reveals a single Cu(II) binding site with coordination somewhat different from that in canonical CopCs, and the absence of a Cu(I) binding site. Extensive bioinformatic analyses indicate that the majority of CopCs in fact contain only a Cu(II) site, with just 10% of sequences corresponding to the canonical two-site CopC. Accordingly, a new classification scheme for CopCs was developed, and detailed analyses of the sequences and their genomic neighborhoods reveal new proteins potentially involved in copper homeostasis, providing a framework for expanded models of CopCD function. PubMed: 27010565DOI: 10.1021/acs.biochem.6b00175 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.46 Å) |
Structure validation
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