ArticleProceedings of the National Academy of Sciences of the United States of America2007
Laboratory evolution of one disulfide isomerase to resemble another.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. 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.
- Bacterial suppressor-of-copper-sensitivity proteins exhibit diverse thiol-disulfide oxidoreductase cellular functions.iScience · 2024Article
- C8J_1298, a bifunctional thiol oxidoreductase of Campylobacter jejuni, affects Dsb (disulfide bond) network functioning.PloS one · 2020Article
- Bacterial thiol oxidoreductases - from basic research to new antibacterial strategies.Applied microbiology and biotechnology · 2017Review
- Sulfur Denitrosylation by an Engineered Trx-like DsbG Enzyme Identifies Nucleophilic Cysteine Hydrogen Bonds as Key Functional Determinant.The Journal of biological chemistry · 2016Article
- Engineering of Helicobacter pylori Dimeric Oxidoreductase DsbK (HP0231).Frontiers in microbiology · 2016Article
- Converting a Sulfenic Acid Reductase into a Disulfide Bond Isomerase.Antioxidants & redox signaling · 2015Article
- Diversity of the Epsilonproteobacteria Dsb (disulfide bond) systems.Frontiers in microbiology · 2015Review
- Identification of disulfide bond isomerase substrates reveals bacterial virulence factors.Molecular microbiology · 2014Article
- Functional and bioinformatics analysis of two Campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, DsbA.PloS one · 2014Article
- Engineered pathways for correct disulfide bond oxidation.Antioxidants & redox signaling · 2011Article
- Mechanisms of oxidative protein folding in the bacterial cell envelope.Antioxidants & redox signaling · 2010Review
- Following evolutionary paths to protein-protein interactions with high affinity and selectivity.Nature structural & molecular biology · 2009Article
- The structure of the bacterial oxidoreductase enzyme DsbA in complex with a peptide reveals a basis for substrate specificity in the catalytic cycle of DsbA enzymes.The Journal of biological chemistry · 2009Article
- Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue.The Journal of biological chemistry · 2009Article
- DSB proteins and bacterial pathogenicity.Nature reviews. Microbiology · 2009Review
- Disulfide bond isomerization in prokaryotes.Biochimica et biophysica acta · 2008Review
- The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner.Molecular microbiology · 2008Article
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It is often difficult to determine which of the sequence and structural differences between divergent members of multigene families are functionally important. Here we use a laboratory evolution approach to determine functionally important structural differences between two distantly related disulfide isomerases, DsbC and DsbG from Escherichia coli. Surprisingly, we found single amino acid substitutions in DsbG that were able to complement dsbC in vivo and have more DsbC-like isomerase activity in vitro. Crystal structures of the three strongest point mutants, DsbG K113E, DsbG V216M, and DsbG T200M, reveal changes in highly surface-exposed regions that cause DsbG to more closely resemble the distantly related DsbC. In this case, laboratory evolution appears to have taken a direct route to allow one protein family member to complement another, with single substitutions apparently bypassing much of the need for multiple changes that took place over approximately 0.5 billion years of evolution. Our findings suggest that, for these two proteins at least, regions important in determining functional differences may represent only a tiny fraction of the overall protein structure.
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