ArticleThe Journal of biological chemistry2011
Oxidation state-dependent protein-protein interactions in disulfide cascades.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- Structure of Arabidopsis SOQ1 lumenal region unveils C-terminal domain essential for negative regulation of photoprotective qH.Nature plants · 2022Article
- Local frustration determines loop opening during the catalytic cycle of an oxidoreductase.eLife · 2020Article
- The Scs disulfide reductase system cooperates with the metallochaperone CueP inThe Journal of biological chemistry · 2019Article
- Structural and biochemical insights into the disulfide reductase mechanism of DsbD, an essential enzyme for neisserial pathogens.The Journal of biological chemistry · 2018Article
- ZnJ2 Is a Member of a Large Chaperone Family in the Chloroplast of Photosynthetic Organisms that Features a DnaJ-Like Zn-Finger Domain.Frontiers in molecular biosciences · 2018Article
- Unconventional Targeting of a Thiol Peroxidase to the Mitochondrial Intermembrane Space Facilitates Oxidative Protein Folding.Cell reports · 2017Article
- An extended active-site motif controls the reactivity of the thioredoxin fold.The Journal of biological chemistry · 2014Article
- 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
- 1H, 13C and 15N resonance assignments for the oxidized and reduced states of the N-terminal domain of DsbD from Escherichia coli.Biomolecular NMR assignments · 2012Article
- The interplay between the disulfide bond formation pathway and cytochrome c maturation in Escherichia coli.FEBS letters · 2012Article
- A pivotal heme-transfer reaction intermediate in cytochrome c biogenesis.The Journal of biological chemistry · 2012Article
- Cytochrome c biogenesis System I.The FEBS journal · 2011Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Bacterial growth and pathogenicity depend on the correct formation of disulfide bonds, a process controlled by the Dsb system in the periplasm of Gram-negative bacteria. Proteins with a thioredoxin fold play a central role in this process. A general feature of thiol-disulfide exchange reactions is the need to avoid a long lived product complex between protein partners. We use a multidisciplinary approach, involving NMR, x-ray crystallography, surface plasmon resonance, mutagenesis, and in vivo experiments, to investigate the interaction between the two soluble domains of the transmembrane reductant conductor DsbD. Our results show oxidation state-dependent affinities between these two domains. These observations have implications for the interactions of the ubiquitous thioredoxin-like proteins with their substrates, provide insight into the key role played by a unique redox partner with an immunoglobulin fold, and are of general importance for oxidative protein-folding pathways in all organisms.
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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.