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Literature summary extracted from

  • Kolberg, M.; Logan, D.T.; Bleifuss, G.; Potsch, S.; Sjoberg, B.M.; Graslund, A.; Lubitz, W.; Lassmann, G.; Lendzian, F.
    A new tyrosyl radical on Phe208 as ligand to the diiron center in Escherichia coli ribonucleotide reductase, mutant R2-Y122H. Combined X-ray diffraction and EPR/ENDOR studies (2005), J. Biol. Chem., 280, 11233-11246.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.17.4.1 mutant Y122H of R2 protein subunit Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
1.17.4.1 Y122H the specific activity of mutant enzyme preparation is less than 0.5% of the wild-type activity. Mutant of R2 protein subunit, the mutant contains a novel stable paramagnetic center, named H. Deteiled characterization of center H, using 1H2H-14N/15N- and 57Fe-EDDOR in comparison with the FeIIIFeIV intermediate X observed in the iron reconstitution reaction of R2, a new tyrosyl radical on Phe208 as ligand to the diiron center Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.17.4.1 Fe2+ each beta-protomer of the small betabeta subunit (R2) contains a binuclear iron cluster with inequivalent binding sites: FeA and FeB. The majority of the protein binds only one Fe(II)atom per betabeta subunit. Additional iron occupation can be achieved upon exposure to O2 or in high glycerol buffers. The binding of the first Fe(II) atom to the active site in a beta-protomer (beta1) induces a global protein conformational change that inhibits access of metal to the active site in the other beta-protomer (betaII). The binding of the same Fe(II) atom also induces a local effect at the active site in beta1-protomer, which lowers the affinity for metal in the A-site Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.17.4.1 Escherichia coli P69924
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-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.4.1 CDP + reduced thioredoxin
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 Escherichia coli 2'-dCDP + thioredoxin disulfide + H2O
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 ?

Synonyms

EC Number Synonyms Comment Organism
1.17.4.1 class I ribonulceotide reductase
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 Escherichia coli
1.17.4.1 RNR
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 Escherichia coli