Cloned (Comment) | Organism |
---|---|
overexpression of DsbC in strain BL21(DE3) | Escherichia coli |
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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
periplasm | - |
Escherichia coli | - |
- |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant DsbC from strain BL21(DE3) by anion exchange chromatography | Escherichia coli |
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 | 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 | 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 | Comment | Organism |
---|---|---|
disulfide-bond isomerase | - |
Escherichia coli |
DsbC | - |
Escherichia coli |
More | the enzyme is a member of the thioredoxin fold superfamily | Escherichia coli |