Article
Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli.
Proceedings of the National Academy of Sciences of the United States of America - 26 Sept 2000
Kadokura H, Bader M, Tian H, Bardwell J C, Beckwith J
Abstract excerpt
The active-site cysteines of DsbA, the periplasmic disulfide-bond-forming enzyme of Escherichia coli, are kept oxidized by the cytoplasmic membrane protein DsbB. DsbB, in turn, is oxidized by two kinds of quinones (ubiquinone for aerobic and menaquinone for anaerobic growth) in the electron-transport chain. We describe the isolation of dsbB missense mutations that change a highly conserved arginine residue at...
Topics
- Amino Acid Sequence
- Arginine
- Bacterial Proteins
- Electron Transport
- Escherichia coli
- Genes, Bacterial
- Membrane Proteins
- Molecular Sequence Data
- Mutation
- Oxidation-Reduction