Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway.

doi:10.1016/j.jmb.2008.01.058

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Article

Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway.

Journal of molecular biology - 11 Apr 2008

Pan Jonathan L, Sliskovic Inga, Bardwell James C A

Abstract excerpt

Disulfide bond formation occurs in secreted proteins in Escherichia coli when the disulfide oxidoreductase DsbA, a soluble periplasmic protein, nonspecifically transfers a disulfide to a substrate protein. The catalytic disulfide of DsbA is regenerated by the inner-membrane protein DsbB. To help identify the specificity determinants in DsbB and to understand the nature of the kinetic barrier preventing direct...

Topics

Bacterial Proteins
Cadmium
Disulfides
Escherichia coli
Escherichia coli Proteins
Glutathione
Isomerism
Membrane Proteins
Models, Molecular
Mutation
Oxidation-Reduction

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Disulfide-Isomerases

Protein Folding

Protein Structure, Secondary

Protein Structure, Tertiary

Signal Transduction

Substrate Specificity

Source

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Identifiers

PMID: 18325532
DOI: 10.1016/j.jmb.2008.01.058
PMCID: PMC2391272

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