IPR028250
Thiol:disulfide interchange protein DsbD, N-terminal domain
InterPro entry
Short name | DsbDN |
Overlapping homologous superfamilies |
Description
Folding of secreted proteins within the periplasm of Escherichia coli requires the formation of disulfide bonds, a process that is dependent on the Dsb (disulfide bond) proteins. The reduction of Dsb proteins DsbC, DsbE, and DsbG occurs by transport of electrons from cytoplasmic thioredoxin to the C-terminal thioredoxin-like domain of DsbD (DsbDC). The N-terminal domain of DsbD (DsbDN) is capable of forming disulfides with oxidized DsbC, DsbE, or DsbG as well as with reduced DsbD
[1]. This entry represents DsbDN
[2].
References
1.Thiol-disulfide exchange in an immunoglobulin-like fold: structure of the N-terminal domain of DsbD. Goulding CW, Sawaya MR, Parseghian A, Lim V, Eisenberg D, Missiakas D. Biochemistry 41, 6920-7, (2002). View articlePMID: 12033924
2.Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis. Smith RP, Whitten AE, Paxman JJ, Kahler CM, Scanlon MJ, Heras B. Acta Crystallogr F Struct Biol Commun 74, 31-38, (2018). PMID: 29372905
Cross References
ENZYME
Contributing Member Database Entry
- Pfam:PF11412
Representative structure
6dnv: Crystal Structure of Neisseria meningitidis DsbD n-terminal domain in the reduced form