PMID:9140064
| Citation |
Kishigami, S and Ito, K (1996) Roles of cysteine residues of DsbB in its activity to reoxidize DsbA, the protein disulphide bond catalyst of Escherichia coli. Genes Cells 1:201-8 |
|---|---|
| Abstract |
DsbA, a periplasmic protein, catalyses the disulphide bond formation of other cell surface proteins in E. coli. Reoxidation of DsbA for catalytic turn over is assured by DsbB, a membrane protein with four essential cysteine residues facing the periplasm. We and others previously reported that the reactive Cys30 residue of DsbA forms a mixed disulphide with DsbB in the absence of its partner Cys33 residue. |
| Links | |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Cysteine/genetics; Cysteine/metabolism; Disulfides/metabolism; Escherichia coli/metabolism; Isomerases/metabolism; Membrane Proteins/genetics; Membrane Proteins/metabolism; Models, Biological; Molecular Sequence Data; Mutation; Oxidation-Reduction; Protein Disulfide-Isomerases |
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