ArticleThe Journal of biological chemistry2009
Role of dimerization in the catalytic properties of the Escherichia coli disulfide isomerase DsbC.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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.
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Who cites it
6 citing papers in PubMed.
- Disulfide bond formation in prokaryotes.Nature microbiology · 2018Review
- Structure of Salmonella FlhE, conserved member of a flagellar type III secretion operon.Journal of molecular biology · 2015Article
- Diversity of the Epsilonproteobacteria Dsb (disulfide bond) systems.Frontiers in microbiology · 2015Review
- The multidrug resistance IncA/C transferable plasmid encodes a novel domain-swapped dimeric protein-disulfide isomerase.The Journal of biological chemistry · 2014Article
- Integrating protein homeostasis strategies in prokaryotes.Cold Spring Harbor perspectives in biology · 2011Review
- Mechanisms of oxidative protein folding in the bacterial cell envelope.Antioxidants & redox signaling · 2010Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The bacterial protein-disulfide isomerase DsbC is a homodimeric V-shaped enzyme that consists of a dimerization domain, two alpha-helical linkers, and two opposing thioredoxin fold catalytic domains. The functional significance of the two catalytic domains of DsbC is not well understood yet. We have engineered heterodimer-like DsbC derivatives covalently linked via (Gly(3)-Ser) flexible linkers. We either inactivated one of the catalytic sites (CGYC), or entirely removed one of the catalytic domains while maintaining the putative binding area intact. Variants having a single active catalytic site display significant levels of isomerase activity. Furthermore, mDsbC[H45D]-dim[D53H], a DsbC variant lacking an entire catalytic domain but with an intact dimerization domain, also showed isomerase activity, albeit at lower levels. In addition, the absence of the catalytic domain allowed this protein to catalyze in vivo oxidation. Our results reveal that two catalytic domains in DsbC are not essential for disulfide bond isomerization and that a determining feature in isomerization is the availability of a substrate binding domain.
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Registered trials
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