Literature summary for 5.3.4.1 extracted from

Yeh, S.M.; Koon, N.; Squire, C.; Metcalf, P.
Structures of the dimerization domains of the Escherichia coli disulfide-bond isomerase enzymes DsbC and DsbG (2007), Acta Crystallogr. Sect. D, 63, 465-471.

Cloned(Commentary)

Cloned (Comment)	Organism
expression of His6-tagged isolated dimerization domains of DsbC and DsbG in strain BL21 (DE3)	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant His6-tagged DsbC and DsbG dimerization domains, sitting drop vapour-diffusion method, 4-6 mg/ml protein in 25 mM HEPES, pH 7.5, 150 mM NaCl, 0.001 ml of protein and of reservoir solution, containing 2.0 M Li2SO4, 0.1 M MgSO4 and 5% 2-propanol, pH 4.5, are mixed, for crystallization of DsbG also addition of 0.2 M CdCl2 and 33% MPD, X-ray diffraction structure determination and analysis at 2.0 and 1.9 A, respectively	Escherichia coli

Crystallization (Comment)

Organism

purified recombinant His6-tagged DsbC and DsbG dimerization domains, sitting drop vapour-diffusion method, 4-6 mg/ml protein in 25 mM HEPES, pH 7.5, 150 mM NaCl, 0.001 ml of protein and of reservoir solution, containing 2.0 M Li2SO4, 0.1 M MgSO4 and 5% 2-propanol, pH 4.5, are mixed, for crystallization of DsbG also addition of 0.2 M CdCl2 and 33% MPD, X-ray diffraction structure determination and analysis at 2.0 and 1.9 A, respectively

Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
periplasm	-	Escherichia coli	-	-

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	isozymes DsbC and DsbG	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His6-tagged isolated dimerization domains of DsbC and DsbG from strain BL21 (DE3) by nickel affinity chromatography and gel filtration	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme shows disulfide reduction and chaperone activities, it facilitates the folding of secreted proteins with multiple disulfide bonds by catalyzing disulfide-bond rearrangement	Escherichia coli	?	-	?

Subunits

Subunits	Comment	Organism
dimer	V-shaped homodimeric modular structures of the dimerization domains and dimer interface of DsbC and DsbG, the dimerization domains fold independently of the catalytic portions of the full-length molecules, overview, 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	Escherichia coli

Synonyms

Synonyms	Comment	Organism
disulfide-bond isomerase	-	Escherichia coli
DsbC	-	Escherichia coli
DsbG	-	Escherichia coli