Abstract
Protein disulfide bond formation is catalyzed by a series of Dsb enzymes present in the periplasm of Escherichia coli. The crystal structure of the DsbB-DsbA-ubiquinone ternary complex provided important insights into mechanisms of the de novo disulfide bond generation cooperated by DsbB and ubiquinone and of the disulfide bond shuttle from DsbB to DsbA. The structural basis for prevention of the crosstalk between the DsbA-DsbB oxidative and the DsbC-DsbD reductive pathways has also been proposed.
| Original language | English |
|---|---|
| Pages (from-to) | 199-201 |
| Number of pages | 3 |
| Journal | Journal of Synchrotron Radiation |
| Volume | 15 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 2008 Apr 18 |
| Externally published | Yes |
Keywords
- Escherichia coli
- Protein disulfide bond generation
ASJC Scopus subject areas
- Radiation
- Nuclear and High Energy Physics
- Instrumentation