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Literature summary for 5.3.4.1 extracted from

  • Kozlov, G.; Maeaettaenen, P.; Schrag, J.D.; Hura, G.L.; Gabrielli, L.; Cygler, M.; Thomas, D.Y.; Gehring, K.
    Structure of the noncatalytic domains and global fold of the protein disulfide isomerase ERp72 (2009), Structure, 17, 651-659.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of b and b' domains and the bb' fragments of ERp57 and ERp72 in Escherichia coli Rattus norvegicus

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant b and b' domains and the bb' fragments of ERp57 and ERp72, hanging drop vapor diffusion method, 0.002 ml protein solution containing 10 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 0.15 M NaCl, and 1 mM DTT, are mixed with 0.002 ml reservoir solution containing 18% w/v PEG MME 2000, 25% glycerol, and 0.1 M Tris, pH 8.0, suspended over 1 ml reservoir solution, 1-3 days, 20°C, X-ray diffraction structure determination and analysis at 1.9 A resolution, overview Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus P38659
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Purification (Commentary)

Purification (Comment) Organism
recombinant b and b' domains and the bb' fragments of ERp57 and ERp72 from Escherichia coli Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information ERp72 substrate specificity of ERp72, overview. Ep72 does not interact with calnexin Rattus norvegicus ?
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?

Subunits

Subunits Comment Organism
More comparison of structures of b and b' domains and the bb' fragments of ERp57 and ERp72, modelling, overview Rattus norvegicus

Synonyms

Synonyms Comment Organism
CaBP2
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Rattus norvegicus
ERp57
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Rattus norvegicus
ERp72
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Rattus norvegicus
protein disulfide isomerase
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Rattus norvegicus
protein disulfide-isomerase A4
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Rattus norvegicus