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 (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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P37146 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
class Ib ribonucleotide reductase | - |
Escherichia coli |
class Ib RNR | - |
Escherichia coli |
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 | 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 |