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Literature summary for 1.17.4.1 extracted from

  • Boal, A.; Cotruvo Jr., J.; Stubbe, J.; Rosenzweig, A.
    Structural basis for activation of class Ib ribonucleotide reductase (2010), Science, 329, 1526-1530.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.17.4.1

Activating Compound

Activating Compound Comment Organism Structure
NrdI involved in binding of FMN. Whereas FeIII 2-tyrosyl radical can self-assemble from FeII 2-NrdF and O2, activation of MnII 2-NrdF requires a reduced flavoprotein, NrdI, proposed to form the oxidant for cofactor assembly by reduction of O2. Lys260 is involved in a hydrogen bond network with the strictly conserved residues Tyr256 and NrdI Glu110, mechanism of MnII 2-NrdF activation by NrdIhq and O2, overview Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
complex between NrdIox and MnII 2-NrdF, Two NrdI and two NrdF molecules are present in the asymmetric unit, X-ray diffraction structure determination and analysis at 2.5 A resolution Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ class Ib ribonucleotide reductase can initiate reduction of nucleotides to deoxynucleotides with either a MnIII 2-tyrosyl radical or a FeIII 2-tyrosyl radical cofactor in the NrdF subunit. Whereas FeIII 2-tyrosyl radical can self-assemble from FeII 2-NrdF and O2, activation of MnII 2-NrdF requires a reduced flavoprotein, NrdI, proposed to form the oxidant for cofactor assembly by reduction of O2 Escherichia coli
Mn2+ class Ib ribonucleotide reductase can initiate reduction of nucleotides to deoxynucleotides with either a MnIII 2-tyrosyl radical or a FeIII 2-tyrosyl radical cofactor in the NrdF subunit. Whereas FeIII 2-tyrosyl radical can self-assemble from FeII 2-NrdF and O2, activation of MnII 2-NrdF requires a reduced flavoprotein, NrdI, proposed to form the oxidant for cofactor assembly by reduction of O2. Structures of MnII 2-NrdF in complex with reduced and oxidized NrdI: a continuous channel connects the NrdI flavin cofactor to the NrdF MnII 2 active site. Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P37146
-
-

Synonyms

Synonyms Comment Organism
class Ib ribonucleotide reductase
-
 Escherichia coli
class Ib RNR
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FMN binding structure analysis with NrdF and NrdI, NrdF contributes to the electrostatic environment of the FMN binding pocket, overview Escherichia coli
additional information class Ib ribonucleotide reductase can initiate reduction of nucleotides to deoxynucleotides with either a MnIII 2-tyrosyl radical or a FeIII 2-tyrosyl radical cofactor in the NrdF subunit. Whereas FeIII 2-tyrosyl radical can self-assemble from FeII 2-NrdF and O2, activation of MnII 2-NrdF requires a reduced flavoprotein, NrdI, proposed to form the oxidant for cofactor assembly by reduction of O2 Escherichia coli

General Information

General Information Comment Organism
physiological function the class Ib ribonucleotide reductase can initiate reduction of nucleotides to deoxynucleotides with either a MnIII 2-tyrosyl radical or a FeIII 2-tyrosyl radical cofactor in the NrdF subunit. Whereas FeIII 2-tyrosyl radical can self-assemble from FeII 2-NrdF and O2, activation of MnII 2-NrdF requires a reduced flavoprotein, NrdI, proposed to form the oxidant for cofactor assembly by reduction of O2 Escherichia coli