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Literature summary for 1.17.4.1 extracted from

  • Larsson, K.M.; Jordan, A.; Eliasson, R.; Reichard, P.; Logan, D.T.; Nordlund, P.
    Structural mechanism of allosteric substrate specificity regulation in a ribonucleotide reductase (2004), Nat. Struct. Mol. Biol., 11, 1142-1149.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop method, crystal structures of the dimeric class II RNR in complex with four cognate allosteric specificity effector-substrate pairs (dTTP-GDP, dGTP-ADP, dATP-CDP or dATP-UDP), as well as structures with only the different effectors (dATP, dTTP or dGTP) Thermotoga maritima

Organism

Organism UniProt Comment Textmining
Thermotoga maritima O33839
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GDP + reduced thioredoxin
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Thermotoga maritima 2'-dGDP + thioredoxin disulfide + H2O
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