ArticleThe EMBO journal2002
The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex.
Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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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.
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Who cites it
47 citing papers in PubMed, 128 citations in OpenAlex.
- Engineering a heme-dependent tryptophan hydroxylase pathway inSynthetic and systems biotechnology · 2026Article
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- Enzymatic basis of the Fc-selective intra-chain disulfide reduction and free thiol content variability in an antibody produced in Escherichia coli.Microbial cell factories · 2022Article
- Protein Disulfide Exchange by the Intramembrane Enzymes DsbB, DsbD, and CcdA.Journal of molecular biology · 2020Review
- Local frustration determines loop opening during the catalytic cycle of an oxidoreductase.eLife · 2020Article
- C8J_1298, a bifunctional thiol oxidoreductase of Campylobacter jejuni, affects Dsb (disulfide bond) network functioning.PloS one · 2020Article
- Disulfide Bond Formation in the Periplasm ofEcoSal Plus · 2019Review
- All Atom Motion Tree detects side chain-related motions and their coupling with domain motion in proteins.Biophysics and physicobiology · 2019Article
- Structural and biochemical insights into the disulfide reductase mechanism of DsbD, an essential enzyme for neisserial pathogens.The Journal of biological chemistry · 2018Article
- Stress control for a well-structured life.The Journal of biological chemistry · 2018Article
- Disulfide isomerase activity of the dynamic, trimericThe Journal of biological chemistry · 2018Article
- A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance.Nature communications · 2017Article
- Expression of a soluble truncated Vargula luciferase in Escherichia coli.Protein expression and purification · 2017Article
- Targeting Bacterial Dsb Proteins for the Development of Anti-Virulence Agents.Molecules (Basel, Switzerland) · 2016Review
- Engineering of Helicobacter pylori Dimeric Oxidoreductase DsbK (HP0231).Frontiers in microbiology · 2016Article
- Single-molecule spectroscopy exposes hidden states in an enzymatic electron relay.Nature communications · 2015Article
- Legionella pneumophila utilizes a single-player disulfide-bond oxidoreductase system to manage disulfide bond formation and isomerization.Molecular microbiology · 2015Article
- Cellular disulfide bond formation in bioactive peptides and proteins.International journal of molecular sciences · 2015Review
- Enzyme structure captures four cysteines aligned for disulfide relay.Protein science : a publication of the Protein Society · 2014Article
- Disulfide bond formation in prokaryotes: history, diversity and design.Biochimica et biophysica acta · 2014Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
Abstract
The Escherichia coli disulfide bond isomerase DsbC rearranges incorrect disulfide bonds during oxidative protein folding. It is specifically activated by the periplasmic N-terminal domain (DsbDalpha) of the transmembrane electron transporter DsbD. An intermediate of the electron transport reaction was trapped, yielding a covalent DsbC-DsbDalpha complex. The 2.3 A crystal structure of the complex shows for the first time the specific interactions between two thiol oxidoreductases. DsbDalpha is a novel thiol oxidoreductase with the active site cysteines embedded in an immunoglobulin fold. It binds into the central cleft of the V-shaped DsbC dimer, which assumes a closed conformation on complex formation. Comparison of the complex with oxidized DsbDalpha reveals major conformational changes in a cap structure that regulates the accessibility of the DsbDalpha active site. Our results explain how DsbC is selectively activated by DsbD using electrons derived from the cytoplasm.
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Registered trials
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.