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Literature summary for 1.13.11.20 extracted from

  • Simmons, C.R.; Liu, Q.; Huang, Q.; Hao, Q.; Begley, T.P.; Karplus, P.A.; Stipanuk, M.H.
    Crystal structure of mammalian cysteine dioxygenase. A novel mononuclear iron center for cysteine thiol oxidation (2006), J. Biol. Chem., 281, 18723-18733.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in BL21(DE3) cells Rattus norvegicus

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallization in sitting drops at 25°C using a reservoir of 0.1-0.25 M ammonium acetate, 0.1 M tri-sodium citrate, pH 5.6, with 22-26% (w/v) polyethylene glycol 4000. The co-crystals with 5 mM are grown using a reservoir of 0.15 M ammonium sulfate, 0.2 M sodium cacodylate, pH 6.5, with 26% (w/v) polyethylene glycol 8000. The crystal sturcture, solved by SAD phasing using selenomethionine-substituted protein, yields a final refined model with r = 18.0 and Rfree = 20.8 at 1.5-A resolution. Data from a co-crystallization experiment with 5 mM cysteine shows structural changes in the binding pocket, they are determined to 1.5 A resolution (final r = 19.8 and Rfree = 22.4). Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
additional information a selenomethionine-substituted cysteine dioxygenase is produced Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus P21816 native and selenomethionine-substituted cysteine dioxygnease
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Posttranslational Modification

Posttranslational Modification Comment Organism
additional information Cys93-Sgamma is covalently bound to Tyr157-Cepsilon2 forming a cysteinyl-tyronsine linkage. Rattus norvegicus

Purification (Commentary)

Purification (Comment) Organism
all buffers are supplemented with 5 mM dithiothreitol to prevent oxidation of the selenomethionine Rattus norvegicus

Synonyms

Synonyms Comment Organism
CDO
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Rattus norvegicus