ArticleAntioxidants & redox signaling2013
Structural and functional characterization of ScsC, a periplasmic thioredoxin-like protein from Salmonella enterica serovar Typhimurium.
Article in Antioxidants & redox signaling, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 27 citations in OpenAlex.
- Bacterial suppressor-of-copper-sensitivity proteins exhibit diverse thiol-disulfide oxidoreductase cellular functions.iScience · 2024Article
- Unveiling the versatility of the thioredoxin framework: Insights from the structural examination ofComputational and structural biotechnology journal · 2024Article
- Making a chink in their armor: Current and next-generation antimicrobial strategies against the bacterial cell envelope.Advances in microbial physiology · 2023Article
- The suppressor of copper sensitivity protein C from Caulobacter crescentus is a trimeric disulfide isomerase that binds copper(I) with subpicomolar affinity.Acta crystallographica. Section D, Structural biology · 2022Article
- Copper Homeostatic Mechanisms and Their Role in the Virulence of Escherichia coli and Salmonella enterica.EcoSal Plus · 2021Review
- Structural bioinformatic analysis of DsbA proteins and their pathogenicity associated substrates.Computational and structural biotechnology journal · 2021Review
- Protein Disulfide Exchange by the Intramembrane Enzymes DsbB, DsbD, and CcdA.Journal of molecular biology · 2020Review
- The Scs disulfide reductase system cooperates with the metallochaperone CueP inThe Journal of biological chemistry · 2019Article
- Engineered variants provide new insight into the structural properties important for activity of the highly dynamic, trimeric protein disulfide isomerase ScsC from Proteus mirabilis.Acta crystallographica. Section D, Structural biology · 2019Article
- The atypical thiol-disulfide exchange protein α-DsbA2 from Wolbachia pipientis is a homotrimeric disulfide isomerase.Acta crystallographica. Section D, Structural biology · 2019Article
- CpxR/CpxA ControlsJournal of bacteriology · 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
- Bacterial thiol oxidoreductases - from basic research to new antibacterial strategies.Applied microbiology and biotechnology · 2017Review
- Structural insight into substrate recognition by the endoplasmic reticulum folding-sensor enzyme: crystal structure of third thioredoxin-like domain of UDP-glucose:glycoprotein glucosyltransferase.Scientific reports · 2014Article
- In-feed use of heavy metal micronutrients in U.S. swine production systems and its role in persistence of multidrug-resistant salmonellae.Applied and environmental microbiology · 2014Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
Abstract
aimsThe prototypical protein disulfide bond (Dsb) formation and protein refolding pathways in the bacterial periplasm involving Dsb proteins have been most comprehensively defined in Escherichia coli. However, genomic analysis has revealed several distinct Dsb-like systems in bacteria, including the pathogen Salmonella enterica serovar Typhimurium. This includes the scsABCD locus, which encodes a system that has been shown via genetic analysis to confer copper tolerance, but whose biochemical properties at the protein level are not defined. The aim of this study was to provide functional insights into the soluble ScsC protein through structural, biochemical, and genetic analyses.
resultsHere we describe the structural and biochemical characterization of ScsC, the soluble DsbA-like component of this system. Our crystal structure of ScsC reveals a similar overall fold to DsbA, although the topology of β-sheets and α-helices in the thioredoxin domains differ. The midpoint reduction potential of the CXXC active site in ScsC was determined to be -132 mV versus normal hydrogen electrode. The reactive site cysteine has a low pKa, typical of the nucleophilic cysteines found in DsbA-like proteins. Deletion of scsC from S. Typhimurium elicits sensitivity to copper (II) ions, suggesting a potential involvement for ScsC in disulfide folding under conditions of copper stress. INNOVATION AND
conclusionScsC is a novel disulfide oxidoreductase involved in protection against copper ion toxicity.
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