Literature summary extracted from
Smith, P.; Zhou, B.; Ho, N.; Yuan, Y.C.; Su, L.; Tsai, S.C.; Yen, Y.
2.6 a X-ray crystal structure of human p53R2, a p53-inducible ribonucleotide reductase (2009), Biochemistry, 48, 11134-11141.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
1.17.4.1 |
P53 |
activates, required |
Homo sapiens |
|
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
1.17.4.1 |
expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) |
Homo sapiens |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
1.17.4.1 |
purified recombinant His6-tagged hp53R2, sitting drop vapor diffusion method, at 25°C, 0.002 ml of 4.5 mg/ml protein in 20 mM Tris, pH 7.5, are mixed with 150 mM NaCl and 0.002 ml of precipitant solution containing 0.1 M sodium citrate, pH 6.45, 1.3 M Li2SO4, and 0.5 M (NH4)2SO4, reservoir volume is 0.250 ml, 7-14 days, addition of ferrous ammonium sulfate of 5 mM 1 h prior to harvesting, X-ray diffraction structure determination and analysis at 2.6 A resolution |
Homo sapiens |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
1.17.4.1 |
deferoxamine mesylate |
an iron chelator |
Homo sapiens |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
1.17.4.1 |
Fe2+ |
monomers A and B exhibit mono- and binuclear iron occupancy, the active site iron coordination environment, involving E131, H134, D100, E194, E228, and H231, is different between monomers A and B, binding structure, overview. Mobility and accessibility of the radical iron center, and radical transfer pathway, overview |
Homo sapiens |
|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
1.17.4.1 |
additional information |
Homo sapiens |
human p53R2 is a 351-residue p53-inducible ribonucleotide reductase small subunit, hp53R2 supplies dNTPs for DNA repair to cells in G0-G1 in a p53-dependent fashion, rather than exhibiting cyclic dNTP synthesis. Hp53R2 structure-function relationship determination and analysis, overview |
? |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.17.4.1 |
Homo sapiens |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
1.17.4.1 |
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration |
Homo sapiens |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.17.4.1 |
additional information |
human p53R2 is a 351-residue p53-inducible ribonucleotide reductase small subunit, hp53R2 supplies dNTPs for DNA repair to cells in G0-G1 in a p53-dependent fashion, rather than exhibiting cyclic dNTP synthesis. Hp53R2 structure-function relationship determination and analysis, overview |
Homo sapiens |
? |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
1.17.4.1 |
More |
one monomer can swivel between two conformations and impose significant influences on helix D and helix B of the opposite monomer. This change ultimately affects the orientation of D100 and, thus, the integrity of the binuclear iron environment. Structural basis of B helix disorder and the N-terminal swivel region, overview |
Homo sapiens |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.17.4.1 |
p53-inducible ribonucleotide reductase |
- |
Homo sapiens |
1.17.4.1 |
RNR |
- |
Homo sapiens |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
1.17.4.1 |
physiological function |
hp53R2 possibly plays a regulatory role in iron assimilation |
Homo sapiens |