Evidence map›Paper›PMID 27010565›Full record

ArticleBiochemistry2016

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

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

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
6.5field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

58 citing papers in PubMed, 107 citations in OpenAlex.

  1. Genome-based identification of heavy metal resistance-associated genes in Bacillus enclensis ABF750 isolated from the polluted sediment of Versova Creek.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026
    Article
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  3. A redox- and proton-coupled inner membrane transporter mediates copper import to the bacterial cytoplasm.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  15. Draft Genome Sequence ofEvolutionary bioinformatics online · 2024
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Thomas J LawtonDepartments of Molecular Biosciences and of Chemistry, Northwestern University , Evanston, Illinois 60208, United States.
Grace E KenneyDepartments of Molecular Biosciences and of Chemistry, Northwestern University , Evanston, Illinois 60208, United States.
Joseph D HurleyDepartments of Molecular Biosciences and of Chemistry, Northwestern University , Evanston, Illinois 60208, United States.
Amy C RosenzweigDepartments of Molecular Biosciences and of Chemistry, Northwestern University , Evanston, Illinois 60208, United States.
Northwestern University · US

Funding

Structure and Specificity in Metal Ion HomeostasisR01GM058518 · NIGMS · NORTHWESTERN UNIVERSITY · PI ROSENZWEIG, AMY C. · 1999 to 2015
$4.4M
Particulate Methane MonooxygenaseR01GM070473 · NIGMS · NORTHWESTERN UNIVERSITY · PI ROSENZWEIG, AMY C. · 2004 to 2015
$3.7M
NCI NIH HHS Y1-CO-1020NIGMS NIH HHS GM58518NIGMS NIH HHS R01 GM058518NIGMS NIH HHS R01 GM070473NIGMS NIH HHS Y1-GM-1104
6 · The paper itself

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.

Indexed as

Bacterial ProteinsCarrier ProteinsComputational BiologyCopperCrystallography, X-RayMethylosinus trichosporiumModels, MolecularMultigene FamilyPeriplasmic Binding ProteinsProtein ConformationProtein Structure, TertiaryStructure-Activity RelationshipBacterial ProteinsCarrier ProteinsCopC protein, BacteriaCoppercopper-binding proteinPeriplasmic Binding Proteins

Identifiers

PMID27010565
PMCPMC5260838
OpenAlexW2303145251

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.