ArticleJournal of molecular biology2010
An extracellular disulfide bond forming protein (DsbF) from Mycobacterium tuberculosis: structural, biochemical, and gene expression analysis.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- Disulfide bonds are required for cell division, cell envelope biogenesis and antibiotic resistance proteins in mycobacteria.bioRxiv : the preprint server for biology · 2025Article
- Computational approaches for molecular characterization and structure-based functional elucidation of a hypothetical protein from Mycobacterium tuberculosis.Genomics & informatics · 2023Article
- Oxidization of TGFβ-activated kinase by MPT53 is required for immunity to Mycobacterium tuberculosis.Nature microbiology · 2019Article
- Identification of the Thioredoxin Partner of Vitamin K Epoxide Reductase in Mycobacterial Disulfide Bond Formation.Journal of bacteriology · 2018Article
- Disulfide bond formation in prokaryotes.Nature microbiology · 2018Review
- Structural analysis of human NHLRC2, mutations of which are associated with FINCA disease.PloS one · 2018Article
- Cmr is a redox-responsive regulator of DosR that contributes to M. tuberculosis virulence.Nucleic acids research · 2017Article
- Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria.Journal of bacteriology · 2015Review
- Structure of a DsbF homologue from Corynebacterium diphtheriae.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Insights into redox sensing metalloproteins in Mycobacterium tuberculosis.Journal of inorganic biochemistry · 2014Review
- Structural and biochemical characterization of the essential DsbA-like disulfide bond forming protein from Mycobacterium tuberculosis.BMC structural biology · 2013Article
- Rv2969c, essential for optimal growth in Mycobacterium tuberculosis, is a DsbA-like enzyme that interacts with VKOR-derived peptides and has atypical features of DsbA-like disulfide oxidases.Acta crystallographica. Section D, Biological crystallography · 2013Article
- Structure analysis of the extracellular domain reveals disulfide bond forming-protein properties of Mycobacterium tuberculosis Rv2969c.Protein & cell · 2013Article
- Analysis of the secretome and identification of novel constituents from culture filtrate of bacillus Calmette-Guerin using high-resolution mass spectrometry.Molecular & cellular proteomics : MCP · 2013Article
- Functional analysis of paralogous thiol-disulfide oxidoreductases in Streptococcus gordonii.The Journal of biological chemistry · 2013Article
- Redox homeostasis in mycobacteria: the key to tuberculosis control?Expert reviews in molecular medicine · 2011Review
- The TB Structural Genomics Consortium: a decade of progress.Tuberculosis (Edinburgh, Scotland) · 2011Review
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Authors and funding
11 authors at 5 institutions in 1 country.
Funding
Abstract
Disulfide bond forming (Dsb) proteins ensure correct folding and disulfide bond formation of secreted proteins. Previously, we showed that Mycobacterium tuberculosis DsbE (Mtb DsbE, Rv2878c) aids in vitro oxidative folding of proteins. Here, we present structural, biochemical, and gene expression analyses of another putative Mtb secreted disulfide bond isomerase protein homologous to Mtb DsbE, Mtb DsbF (Rv1677). The X-ray crystal structure of Mtb DsbF reveals a conserved thioredoxin fold although the active-site cysteines may be modeled in both oxidized and reduced forms, in contrast to the solely reduced form in Mtb DsbE. Furthermore, the shorter loop region in Mtb DsbF results in a more solvent-exposed active site. Biochemical analyses show that, similar to Mtb DsbE, Mtb DsbF can oxidatively refold reduced, unfolded hirudin and has a comparable pK(a) for the active-site solvent-exposed cysteine. However, contrary to Mtb DsbE, the Mtb DsbF redox potential is more oxidizing and its reduced state is more stable. From computational genomics analysis of the M. tuberculosis genome, we identified a potential Mtb DsbF interaction partner, Rv1676, a predicted peroxiredoxin. Complex formation is supported by protein coexpression studies and inferred by gene expression profiles, whereby Mtb DsbF and Rv1676 are upregulated under similar environments. Additionally, comparison of Mtb DsbF and Mtb DsbE gene expression data indicates anticorrelated gene expression patterns, suggesting that these two proteins and their functionally linked partners constitute analogous pathways that may function under different conditions.
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