2IYJ

Crystal structure of the N-terminal dimer domain of E.coli DsbC

Summary for 2IYJ

• Entry DOI: 10.2210/pdb2iyj/pdb
• Related: 1EEJ 1G0T 1JZD 1JZO 1TJD
• Descriptor: THIOL DISULFIDE INTERCHANGE PROTEIN DSBC, SULFATE ION (3 entities in total)
• Functional Keywords: disulfide bond isomerase, isomerase, dsbc, dsbg, periplasmic, redox-active center
• Biological source: ESCHERICHIA COLI
• Cellular location: Periplasm: P0AEG6
• Total number of polymer chains: 2
• Total formula weight: 15964.31

Authors

Yeh, S.-M.,Metcalf, P. (deposition date: 2006-07-18, release date: 2007-07-24, Last modification date: 2023-12-13)

Primary citation

Yeh, S.-M.,Koon, N.,Squire, C.,Metcalf, P.
Structures of Dimerization Domains of the Escherichia Coli Disulfide-Bond Isomerase Enzymes Dsbc and Dsbg.
Acta Crystallogr.,Sect.D, 63:465-, 2007

PubMed Abstract: DsbC and DsbG are periplasmic disulfide-bond isomerases, enzymes that facilitate the folding of secreted proteins with multiple disulfide bonds by catalyzing disulfide-bond rearrangement. Both enzymes also have in vitro chaperone activity. The crystal structures of these molecules are similar and both are V-shaped homodimeric modular structures. Each dimeric molecule contains two separate C-terminal thioredoxin-fold domains, joined by hinged helical "stalks" to a single N-terminal dimerization domain formed from the N-terminal 67 residues of each monomer. In this work, the crystal structures of the separate DsbC and DsbG dimerization domains have been determined at resolutions of 2.0 and 1.9 A, respectively. The two structures are both similar to the corresponding domains in the full-length molecules, showing that the dimerization domains fold independently of the catalytic portions of the full-length molecules. Localized structural differences between DsbC and DsbG were observed near the dimer interface and may be relevant to the different functions of the two enzymes.

PubMed: 17372350
DOI: 10.1107/S0907444907003320

Experimental method

X-RAY DIFFRACTION (2 Å)