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Literature summary for 5.3.4.1 extracted from

  • Banaszak, K.; Mechin, I.; Frost, G.; Rypniewski, W.
    Structure of the reduced disulfide-bond isomerase DsbC from Escherichia coli (2004), Acta Crystallogr. Sect. D, 60, 1747-1752.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of DsbC in strain BL21(DE3) Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant reduced DsbC, hanging drop vapour diffusion method, the reservoir solution contains 0.2 M Li2SO4, o.1 M Tris, pH8.4, and 20% PEG 4000, 0.0015 ml of protein and of reservoir solution are mixed, X-ray diffraction reduced structure determination and analysis at 2.5 A resolution Escherichia coli

Localization

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli the enzyme plays a crucial role in folding periplasmatically excreted proteins ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant DsbC from strain BL21(DE3) by anion exchange chromatography Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
catalyses the rearrangement of -S-S- bonds in proteins structure of oxidized and reduced active site, the active site motif is -C-X-X-C- Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme plays a crucial role in folding periplasmatically excreted proteins Escherichia coli ?
-
?
additional information Cys98 and Cys101 form the reversible disulfide bond in the active site, the enzyme is active in reduced state which is stabilized by hydrogen bond interactions of the active cysteine residues with Thr94 and Thr182 Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
dimer DsbC contains an N-terminal dimerization domain followed by a linker helix both involved in protein dimerization, the linker helix helps separate the C-terminal catalytic domains Escherichia coli

Synonyms

Synonyms Comment Organism
disulfide-bond isomerase
-
Escherichia coli
DsbC
-
Escherichia coli
More the enzyme is a member of the thioredoxin fold superfamily Escherichia coli