The CopC Family: Structural and Bioinformatic Insights into a Diverse Group of Periplasmic Copper Binding Proteins

Lawton, Thomas J.; Kenney, Grace E.; Hurley, Joseph D.; Rosenzweig, Amy C.

doi:10.1021/acs.biochem.6b00175

Title: The CopC Family: Structural and Bioinformatic Insights into a Diverse Group of Periplasmic Copper Binding Proteins

Journal Article · Wed Apr 06 00:00:00 EDT 2016 · Biochemistry

DOI:https://doi.org/10.1021/acs.biochem.6b00175· OSTI ID:1249255

Lawton, Thomas J. ^[1]; Kenney, Grace E. ^[1]; Hurley, Joseph D. ^[1]; Rosenzweig, Amy C. ^[1]

Northwestern Univ., Evanston, IL (United States)

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. Furthermore, 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.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: USDOE Office of Science (SC); Michigan Economic Development Corp. and Michigan Technology Tri-Corridor Grant; National Institutes of Health (NIH); National Cancer Institute (NCI); National Institute of General Medical Sciences (NIGMS); American Heart Association Predoctoral Fellowship; Northwestern University Undergraduate Research Grant

Grant/Contract Number:: AC02-06CH11357; 085P1000817; Y1-CO-1020; Y1-GM-1104; GM58518

OSTI ID:: 1249255

Journal Information:: Biochemistry, Vol. 55, Issue 15; ISSN 0006-2960

Publisher:: American Chemical Society (ACS)Copyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 54 works

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