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Literature summary extracted from

  • Furlong, E.J.; Kurth, F.; Premkumar, L.; Whitten, A.E.; Martin, J.L.
    Engineered variants provide new insight into the structural properties important for activity of the highly dynamic, trimeric protein disulfide isomerase ScsC from Proteus mirabilis (2019), Acta Crystallogr. Sect. D, 75, 296-307.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.3.4.1 expressed in Escherichia coli BL21(DE3) pLysS cells Proteus mirabilis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.3.4.1 N-terminally truncated form of the protomer with two helices of the trimerization stem removed, generating a protein with dithiol oxidase rather than disulfide isomerase activity, hanging drop vapor diffusion method, using 0.1 M HEPES pH 7, 32%(v/v) Jeffamine M-600 Proteus mirabilis

Organism

EC Number Organism UniProt Comment Textmining
5.3.4.1 Proteus mirabilis B4EV21
-
-
5.3.4.1 Proteus mirabilis HI4320 B4EV21
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.3.4.1 immobilized metal affinity chromatography and gel filtration Proteus mirabilis

Subunits

EC Number Subunits Comment Organism
5.3.4.1 trimer small angle X-ray scattering Proteus mirabilis

Synonyms

EC Number Synonyms Comment Organism
5.3.4.1 protein disulfide isomerase
-
 Proteus mirabilis
5.3.4.1 ScsC
-
 Proteus mirabilis
5.3.4.1 suppressor of copper sensitivity protein C
-
 Proteus mirabilis

General Information

EC Number General Information Comment Organism
5.3.4.1 physiological function the enzyme plays a role in copper tolerance Proteus mirabilis