1JZO

DsbC C101S

Summary for 1JZO

• Entry DOI: 10.2210/pdb1jzo/pdb
• Related: 1JZD 1eej
• Descriptor: THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC (2 entities in total)
• Functional Keywords: disulfide bond isomerase, thiol oxidoreductase, dsbc, thioredoxin fold, oxidoreductase
• Biological source: Escherichia coli
• Cellular location: Periplasm: P21892
• Total number of polymer chains: 2
• Total formula weight: 46943.90

Authors

Haebel, P.W.,Goldstone, D.,Katzen, F.,Beckwith, J.,Metcalf, P. (deposition date: 2001-09-17, release date: 2003-03-08, Last modification date: 2024-11-06)

Primary citation

Haebel, P.W.,Goldstone, D.,Katzen, F.,Beckwith, J.,Metcalf, P.
The Disulfide Bond Isomerase DsbC is Activated by an Immunoglobulin-fold Thiol Oxidoreductase: Crystal Structure of the DsbC-DsbDalpha complex.
Embo J., 21:4774-4784, 2002

PubMed Abstract: The Escherichia coli disulfide bond isomerase DsbC rearranges incorrect disulfide bonds during oxidative protein folding. It is specifically activated by the periplasmic N-terminal domain (DsbDalpha) of the transmembrane electron transporter DsbD. An intermediate of the electron transport reaction was trapped, yielding a covalent DsbC-DsbDalpha complex. The 2.3 A crystal structure of the complex shows for the first time the specific interactions between two thiol oxidoreductases. DsbDalpha is a novel thiol oxidoreductase with the active site cysteines embedded in an immunoglobulin fold. It binds into the central cleft of the V-shaped DsbC dimer, which assumes a closed conformation on complex formation. Comparison of the complex with oxidized DsbDalpha reveals major conformational changes in a cap structure that regulates the accessibility of the DsbDalpha active site. Our results explain how DsbC is selectively activated by DsbD using electrons derived from the cytoplasm.

PubMed: 12234918
DOI: 10.1093/emboj/cdf489

Experimental method

X-RAY DIFFRACTION (1.92 Å)