› 2av8

X-ray diffraction
2.46Å resolution

Y122F MUTANT OF RIBONUCLEOTIDE REDUCTASE FROM ESCHERICHIA COLI

Released:
DOI: 10.2210/pdb2av8/pdb
PDB entry 2av8 coloured by chain, front view.
PDB entry 2av8 coloured by chain, side view.
PDB entry 2av8 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Characterization of Y122F R2 of Escherichia coli ribonucleotide reductase by time-resolved physical biochemical methods and X-ray crystallography.
Tong W, Burdi D, Riggs-Gelasco P, Chen S, Edmondson D, Huynh BH, Stubbe J, Han S, Arvai A, Tainer J
Biochemistry 37 5840-8 (1998)
PMID: 9558317

Function and Biology Details

Reaction catalysed: 
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159694 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonucleoside-diphosphate reductase 1 subunit beta Chains: A, B
Molecule details ›
Chains: A, B
Length: 340 amino acids
Theoretical weight: 39.59 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P69924 (Residues: 2-341; Coverage: 90%)
Gene names: JW2229, b2235, ftsB, nrdB
Sequence domains: Ribonucleotide reductase, small chain
Structure domains: Ribonucleotide Reductase, subunit A

Ligands and Environments

2 bound ligands:
Ligand FE2 1 x FE2
Ligand FEO 2 x FEO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P61
Unit cell:
a: 136.5Å b: 136.5Å c: 109.6Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.181 0.181 0.237
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Structure and function of the radical enzyme ribonucleotide reductase.
Eklund et al. (2001)
5 more

2 mentions without citation

Novel mutator mutants of E. coli nrdAB ribonucleotide reductase: insight into allosteric regulation and control of mutation rates.
Ahluwalia et al. (2012)
1 more