ArticleThe Journal of biological chemistry2009
Crystal structure and biophysical properties of Bacillus subtilis BdbD. An oxidizing thiol:disulfide oxidoreductase containing a novel metal site.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 43 citations in OpenAlex.
- Structural and functional specialization of Bordetella pertussis DsbA for pertussis toxin folding.Protein science : a publication of the Protein Society · 2026Article
- Protein trafficking across the cell envelope of gram-positive bacteria.Journal of bacteriology · 2025Review
- Disulphide bond-forming enzymes in clostridial species.Microbiology (Reading, England) · 2025Article
- A cryptic oxidoreductase safeguards oxidative protein folding inProceedings of the National Academy of Sciences of the United States of America · 2023Article
- A Buried Water Network Modulates the Activity of theAntioxidants (Basel, Switzerland) · 2023Article
- Diversity of CytochromeMicroorganisms · 2022Review
- Thiol Reductases inAntioxidants (Basel, Switzerland) · 2022Review
- Identification of a Thiol-Disulfide Oxidoreductase (SdbA) Catalyzing Disulfide Bond Formation in the Superantigen SpeA in Streptococcus pyogenes.Journal of bacteriology · 2021Article
- Structural bioinformatic analysis of DsbA proteins and their pathogenicity associated substrates.Computational and structural biotechnology journal · 2021Review
- Inhibition of Diverse DsbA Enzymes in Multi-DsbA Encoding Pathogens.Antioxidants & redox signaling · 2018Article
- Forespore Targeting of SpoVD in Bacillus subtilis Is Mediated by the N-Terminal Part of the Protein.Journal of bacteriology · 2018Article
- Disulfide bond formation in prokaryotes.Nature microbiology · 2018Review
- Bifunctionality of a biofilm matrix protein controlled by redox state.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structural and Biochemical Characterization of Chlamydia trachomatis DsbA Reveals a Cysteine-Rich and Weakly Oxidising Oxidoreductase.PloS one · 2016Article
- A thiol-disulfide oxidoreductase of the Gram-positive pathogen Corynebacterium diphtheriae is essential for viability, pilus assembly, toxin production and virulence.Molecular microbiology · 2015Article
- A Disulfide Bond-forming Machine Is Linked to the Sortase-mediated Pilus Assembly Pathway in the Gram-positive Bacterium Actinomyces oris.The Journal of biological chemistry · 2015Article
- Crystal Structure of DsbA from Corynebacterium diphtheriae and Its Functional Implications for CueP in Gram-Positive Bacteria.Molecules and cells · 2015Article
- Structure of a DsbF homologue from Corynebacterium diphtheriae.Acta crystallographica. Section F, Structural biology communications · 2014Article
- An extended active-site motif controls the reactivity of the thioredoxin fold.The Journal of biological chemistry · 2014Article
- Structural and functional characterization of ScsC, a periplasmic thioredoxin-like protein from Salmonella enterica serovar Typhimurium.Antioxidants & redox signaling · 2013Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
BdbD is a thiol:disulfide oxidoreductase (TDOR) from Bacillus subtilis that functions to introduce disulfide bonds in substrate proteins/peptides on the outside of the cytoplasmic membrane and, as such, plays a key role in disulfide bond management. Here we demonstrate that the protein is membrane-associated in B. subtilis and present the crystal structure of the soluble part of the protein lacking its membrane anchor. This reveals that BdbD is similar in structure to Escherichia coli DsbA, with a thioredoxin-like domain with an inserted helical domain. A major difference, however, is the presence in BdbD of a metal site, fully occupied by Ca(2+), at an inter-domain position some 14 A away from the CXXC active site. The midpoint reduction potential of soluble BdbD was determined as -75 mV versus normal hydrogen electrode, and the active site N-terminal cysteine thiol was shown to have a low pK(a), consistent with BdbD being an oxidizing TDOR. Equilibrium unfolding studies revealed that the oxidizing power of the protein is based on the instability introduced by the disulfide bond in the oxidized form. The crystal structure of Ca(2+)-depleted BdbD showed that the protein remained folded, with only minor conformational changes. However, the reduced form of Ca(2+)-depleted BdbD was significantly less stable than reduced Ca(2+)-containing protein, and the midpoint reduction potential was shifted by approximately -20 mV, suggesting that Ca(2+) functions to boost the oxidizing power of the protein. Finally, we demonstrate that electron exchange does not occur between BdbD and B. subtilis ResA, a low potential extra-cytoplasmic TDOR.
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