Article
Identification of a segment of DsbB essential for its respiration-coupled oxidation.
Molecular microbiology - 1 Jan 2001
Kobayashi T, Takahashi Y, Ito K
Abstract excerpt
In the Escherichia coli protein disulphide bond formation pathway, membrane-bound DsbB oxidizes periplasmic DsbA, the disulphide bond-introducing enzyme. The Cys-41-Val-Leu-Cys-44 motif in the first periplasmic domain of DsbB is kept strongly oxidized by the respiratory function of the cell. We now show that the characteristic dithiothreitol resistance of the Cys-41-Cys-44 bond was retained even when the flanked...
Topics
- Amino Acid Sequence
- Bacterial Proteins
- Dithiothreitol
- Drug Resistance, Microbial
- Membrane Proteins
- Molecular Sequence Data
- Mutagenesis, Insertional
- Mutation
- Oxidation-Reduction
- Oxidoreductases
- Oxygen Consumption