ArticlePloS one2014
CorA is a copper repressible surface-associated copper(I)-binding protein produced in Methylomicrobium album BG8.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- Prolific S-layer shedding and associated proteins from the methanotrophApplied and environmental microbiology · 2026Article
- Extrinsic and intrinsic factors affect copper-induced protein precipitation across eukaryotic and prokaryotic proteomes.Protein science : a publication of the Protein Society · 2025Article
- BR-Bodies Facilitate Adaptive Responses and Survival During Copper Stress inbioRxiv : the preprint server for biology · 2025Article
- Microbial hauberks: composition and function of surface layer proteins in gammaproteobacterial methanotrophs.Applied and environmental microbiology · 2025Article
- Methanobactins: Structures, Biosynthesis, and Microbial Diversity.Annual review of microbiology · 2024Review
- Direct Methane Oxidation by Copper- and Iron-Dependent Methane Monooxygenases.Chemical reviews · 2024Review
- Copper binding by a unique family of metalloproteins is dependent on kynurenine formation.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- MbnH is a diheme MauG-like protein associated with microbial copper homeostasis.The Journal of biological chemistry · 2019Article
- Aerobic methane oxidation under copper scarcity in a stratified lake.Scientific reports · 2019Article
- Chalkophores.Annual review of biochemistry · 2018Review
- Rare Earth Elements Alter Redox Balance inFrontiers in microbiology · 2018Article
- Methanobactins: from genome to function.Metallomics : integrated biometal science · 2017Review
- Methanobactin and the Link between Copper and Bacterial Methane Oxidation.Microbiology and molecular biology reviews : MMBR · 2016Review
- Tripping up Trp: Modification of protein tryptophan residues by reactive oxygen species, modes of detection, and biological consequences.Free radical biology & medicine · 2015Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
CorA is a copper repressible protein previously identified in the methanotrophic bacterium Methylomicrobium album BG8. In this work, we demonstrate that CorA is located on the cell surface and binds one copper ion per protein molecule, which, based on X-ray Absorption Near Edge Structure analysis, is in the reduced state (Cu(I)). The structure of endogenously expressed CorA was solved using X-ray crystallography. The 1.6 Å three-dimensional structure confirmed the binding of copper and revealed that the copper atom was coordinated in a mononuclear binding site defined by two histidines, one water molecule, and the tryptophan metabolite, kynurenine. This arrangement of the copper-binding site is similar to that of its homologous protein MopE* from Metylococcus capsulatus Bath, confirming the importance of kynurenine for copper binding in these proteins. Our findings show that CorA has an overall fold similar to MopE, including the unique copper(I)-binding site and most of the secondary structure elements. We suggest that CorA plays a role in the M. album BG8 copper acquisition.
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