Conversion of a catalytic into a structural disulfide bond by circular permutation.

doi:10.1021/bi981888v

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Article

Conversion of a catalytic into a structural disulfide bond by circular permutation.

Biochemistry - 15 Dec 1998

Hennecke J, Glockshuber R

Abstract excerpt

The thiol-disulfide oxidoreductase DsbA from Escherichia coli is the strongest oxidant of the enzyme family and required for disulfide bond formation in the bacterial periplasm. The catalytic domain of this 189-residue protein has a thioredoxin-like fold and contains a catalytic disulfide bridge...

Topics

Catalysis
Disulfides
Escherichia coli
Histidine
Mutagenesis, Site-Directed
Oxidation-Reduction
Phenotype
Plasmids
Proline
Protein Conformation
Protein Disulfide-Isomerases
Protein Folding
Thermodynamics

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