ArticleThe EMBO journal2007
Redox-active cysteines of a membrane electron transporter DsbD show dual compartment accessibility.
Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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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.
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.
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Who cites it
25 citing papers in PubMed, 49 citations in OpenAlex.
- Giant viruses encode vitamin K-based redox modules for lipid modification.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Article
- Protein Disulfide Exchange by the Intramembrane Enzymes DsbB, DsbD, and CcdA.Journal of molecular biology · 2020Review
- The mammalian cytosolic thioredoxin reductase pathway acts via a membrane protein to reduce ER-localised proteins.Journal of cell science · 2020Article
- Distinct Roles of Shewanella oneidensis Thioredoxin in Regulation of Cellular Responses to Hydrogen and Organic Peroxides.Applied and environmental microbiology · 2019Article
- Disulfide Bond Formation in the Periplasm ofEcoSal Plus · 2019Review
- Solution structure and elevator mechanism of the membrane electron transporter CcdA.Nature structural & molecular biology · 2018Article
- Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Targeting Bacterial Dsb Proteins for the Development of Anti-Virulence Agents.Molecules (Basel, Switzerland) · 2016Review
- Structure and multistate function of the transmembrane electron transporter CcdA.Nature structural & molecular biology · 2015Article
- Helicobacter pylori HP0377, a member of the Dsb family, is an untypical multifunctional CcmG that cooperates with dimeric thioldisulfide oxidase HP0231.BMC microbiology · 2015Article
- Cellular disulfide bond formation in bioactive peptides and proteins.International journal of molecular sciences · 2015Review
- Structures of an intramembrane vitamin K epoxide reductase homolog reveal control mechanisms for electron transfer.Nature communications · 2014Article
- Review
- Disulfide bond formation in the bacterial periplasm: major achievements and challenges ahead.Antioxidants & redox signaling · 2013Review
- Many roles of the bacterial envelope reducing pathways.Antioxidants & redox signaling · 2013Review
- Disulfide bond formation in the mammalian endoplasmic reticulum.Cold Spring Harbor perspectives in biology · 2012Review
- Article
- A comparison of the endotoxin biosynthesis and protein oxidation pathways in the biogenesis of the outer membrane of Escherichia coli and Neisseria meningitidis.Frontiers in cellular and infection microbiology · 2012Review
- TrbB from conjugative plasmid F is a structurally distinct disulfide isomerase that requires DsbD for redox state maintenance.Journal of bacteriology · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The membrane-embedded domain of the unusual electron transporter DsbD (DsbDbeta) uses two redox-active cysteines to catalyze electron transfer between thioredoxin-fold polypeptides on opposite sides of the bacterial cytoplasmic membrane. How the electrons are transferred across the membrane is unknown. Here, we show that DsbDbeta displays an inherent functional and structural symmetry: first, the two cysteines of DsbDbeta can be alkylated from both the cytoplasm and the periplasm. Second, when the two cysteines are disulfide-bonded, cysteine scanning shows that the C-terminal halves of the cysteine-containing transmembrane segments 1 and 4 are exposed to the aqueous environment while the N-terminal halves are not. Third, proline residues located pseudo-symmetrically around the two cysteines are required for redox activity and accessibility of the cysteines. Fourth, mixed disulfide complexes, apparent intermediates in the electron transfer process, are detected between DsbDbeta and thioredoxin molecules on each side of the membrane. We propose a model where the two redox-active cysteines are located at the center of the membrane, accessible on both sides of the membrane to the thioredoxin proteins.
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What OpenQuestion holds
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.