ArticleBiochemistry2009
Structure and function of Bacillus subtilis YphP, a prokaryotic disulfide isomerase with a CXC catalytic motif .
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 35 citations in OpenAlex.
- Suppression of Thiol-Dependent Antioxidant System and Stress Response in Methicillin-Resistant Staphylococcus aureus by Docosanol: Explication Through Proteome Investigation.Molecular biotechnology · 2022Article
- Structure of BrxA from Staphylococcus aureus, a bacilliredoxin involved in redox homeostasis in Firmicutes.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Redox chemistry of lens crystallins: A system of cysteines.Experimental eye research · 2021Review
- Thiol-Mediated Uptake.JACS Au · 2021Review
- Inhibitors of thiol-mediated uptake.Chemical science · 2020Article
- Comparative differential cuproproteomes of Rhodobacter capsulatus reveal novel copper homeostasis related proteins.Metallomics : integrated biometal science · 2020Article
- Contribution of YjbIH to Virulence Factor Expression and Host Colonization inInfection and immunity · 2019Article
- Redox regulation by reversible protein S-thiolation in Gram-positive bacteria.Redox biology · 2019Review
- Dynamic disulfide exchange in a crystallin protein in the human eye lens promotes cataract-associated aggregation.The Journal of biological chemistry · 2018Article
- The Role of Bacillithiol in Gram-Positive Firmicutes.Antioxidants & redox signaling · 2018Review
- Redox regulation by reversible protein S-thiolation in bacteria.Frontiers in microbiology · 2015Review
- Redox regulation in Bacillus subtilis: The bacilliredoxins BrxA(YphP) and BrxB(YqiW) function in de-bacillithiolation of S-bacillithiolated OhrR and MetE.Antioxidants & redox signaling · 2014Article
- Biophysical features of bacillithiol, the glutathione surrogate of Bacillus subtilis and other firmicutes.Chembiochem : a European journal of chemical biology · 2013Article
- S-bacillithiolation protects conserved and essential proteins against hypochlorite stress in firmicutes bacteria.Antioxidants & redox signaling · 2013Article
- Contributions of a disulfide bond and a reduced cysteine side chain to the intrinsic activity of the high-density lipoprotein receptor SR-BI.Biochemistry · 2012Article
- Twin disulfides for orthogonal disulfide pairing and the directed folding of multicyclic peptides.Nature chemistry · 2012Article
- Role of N-glycosylation sites and CXC motifs in trafficking of medicago truncatula Nod factor perception protein to plasma membrane.The Journal of biological chemistry · 2012Article
- New role of the disulfide stress effector YjbH in β-lactam susceptibility of Staphylococcus aureus.Antimicrobial agents and chemotherapy · 2011Article
- S-bacillithiolation protects against hypochlorite stress in Bacillus subtilis as revealed by transcriptomics and redox proteomics.Molecular & cellular proteomics : MCP · 2011Article
- Atomic resolution insights into curli fiber biogenesis.Structure (London, England : 1993) · 2011Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
The DUF1094 family contains over 100 bacterial proteins, all containing a conserved CXC motif, with unknown function. We solved the crystal structure of the Bacillus subtilis representative, the product of the yphP gene. The protein shows remarkable structural similarity to thioredoxins, with a canonical alphabetaalphabetaalphabetabetaalpha topology, despite low amino acid sequence identity to thioredoxin. The CXC motif is found in the loop immediately downstream of the first beta-strand, in a location equivalent to the CXXC motif of thioredoxins, with the first Cys occupying a position equivalent to the first Cys in canonical thioredoxin. The experimentally determined reduction potential of YphP is E degrees' = -130 mV, significantly higher than that of thioredoxin and consistent with disulfide isomerase activity. Functional assays confirmed that the protein displays a level of isomerase activity that might be biologically significant. We propose a mechanism by which the members of this family catalyze isomerization using the CXC catalytic site.
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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.