1UC7

Crystal structure of DsbDgamma

Summary for 1UC7

• Entry DOI: 10.2210/pdb1uc7/pdb
• Descriptor: Thiol:disulfide interchange protein dsbD (2 entities in total)
• Functional Keywords: thioredoxin-fold, oxidoreductase
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Multi-pass membrane protein (By similarity): P58162
• Total number of polymer chains: 2
• Total formula weight: 27917.44

Authors

Kim, J.H.,Kim, S.J.,Jeong, D.G.,Son, J.H.,Ryu, S.E. (deposition date: 2003-04-09, release date: 2004-04-27, Last modification date: 2024-10-23)

Primary citation

Kim, J.H.,Kim, S.J.,Jeong, D.G.,Son, J.H.,Ryu, S.E.
Crystal structure of DsbDgamma reveals the mechanism of redox potential shift and substrate specificity(1)
FEBS LETT., 543:164-169, 2003

PubMed Abstract: The Escherichia coli transmembrane protein DsbD transfers electrons from the cytoplasm to the periplasm through a cascade of thiol-disulfide exchange reactions. In this process, the C-terminal periplasmic domain of DsbD (DsbDgamma) shuttles the reducing potential from the membrane domain (DsbDbeta) to the N-terminal periplasmic domain (DsbDalpha). The crystal structure of DsbDgamma determined at 1.9 A resolution reveals that the domain has a thioredoxin fold with an extended N-terminal stretch. In comparison to thioredoxin, the DsbDgamma structure exhibits the stabilized active site conformation and the extended active site alpha2 helix that explain the domain's substrate specificity and the redox potential shift, respectively. The hypothetical model of the DsbDgamma:DsbDalpha complex based on the DsbDgamma structure and previous structural studies indicates that the conserved hydrophobic residue in the C-X-X-C motif of DsbDgamma may be important in the specific recognition of DsbDalpha.

PubMed: 12753926
DOI: 10.1016/S0014-5793(03)00434-4

Experimental method

X-RAY DIFFRACTION (1.9 Å)