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

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. 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 proteinsmore » potentially involved in copper homeostasis, providing a framework for expanded models of CopCD function.« less

Authors:
 [1];  [1];  [1];  [1]
  1. Northwestern Univ., Evanston, IL (United States)
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
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
OSTI Identifier:
1249255
Grant/Contract Number:  
AC02-06CH11357; 085P1000817; Y1-CO-1020; Y1-GM-1104; GM58518
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Biochemistry
Additional Journal Information:
Journal Volume: 55; Journal Issue: 15; Journal ID: ISSN 0006-2960
Publisher:
American Chemical Society (ACS)
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; Peptides and proteins; Copper; Monomers; Genomics; Screening assays

Citation Formats

Lawton, Thomas J., Kenney, Grace E., Hurley, Joseph D., and Rosenzweig, Amy C. The CopC Family: Structural and Bioinformatic Insights into a Diverse Group of Periplasmic Copper Binding Proteins. United States: N. p., 2016. Web. doi:10.1021/acs.biochem.6b00175.
Lawton, Thomas J., Kenney, Grace E., Hurley, Joseph D., & Rosenzweig, Amy C. The CopC Family: Structural and Bioinformatic Insights into a Diverse Group of Periplasmic Copper Binding Proteins. United States. doi:10.1021/acs.biochem.6b00175.
Lawton, Thomas J., Kenney, Grace E., Hurley, Joseph D., and Rosenzweig, Amy C. Wed . "The CopC Family: Structural and Bioinformatic Insights into a Diverse Group of Periplasmic Copper Binding Proteins". United States. doi:10.1021/acs.biochem.6b00175. https://www.osti.gov/servlets/purl/1249255.
@article{osti_1249255,
title = {The CopC Family: Structural and Bioinformatic Insights into a Diverse Group of Periplasmic Copper Binding Proteins},
author = {Lawton, Thomas J. and Kenney, Grace E. and Hurley, Joseph D. and Rosenzweig, Amy C.},
abstractNote = {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.},
doi = {10.1021/acs.biochem.6b00175},
journal = {Biochemistry},
issn = {0006-2960},
number = 15,
volume = 55,
place = {United States},
year = {2016},
month = {4}
}

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Works referencing / citing this record:

Characterization of a long overlooked copper protein from methane- and ammonia-oxidizing bacteria
journal, October 2018