Article
Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity.
The EMBO journal - 15 Apr 1994
Shevchik V E, Condemine G, Robert-Baudouy J
Abstract excerpt
We identified and characterized an Erwinia chrysanthemi gene able to complement an Escherichia coli dsbA mutation that prevents disulfide bond formation in periplasmic proteins. This gene, dsbC, codes for a 24 kDa periplasmic protein that contains a characteristic active site sequence of disulfid...
Topics
- Amino Acid Sequence
- Base Sequence
- Cell Compartmentation
- Cloning, Molecular
- Dickeya chrysanthemi
- Escherichia coli
- Genes, Bacterial
- Genetic Complementation Test
- Isomerases
- Membrane Proteins
- Molecular Sequence Data
- Mutation
- Protein Disulfide-Isomerases
- Sequence Analysis, DNA
- Sequence Homology, Amino Acid