› 1l1l

X-ray diffraction
1.75Å resolution

CRYSTAL STRUCTURE OF B-12 DEPENDENT (CLASS II) RIBONUCLEOTIDE REDUCTASE

Released:
DOI: 10.2210/pdb1l1l/pdb
PDB entry 1l1l coloured by chain, front view.
PDB entry 1l1l coloured by chain, side view.
PDB entry 1l1l coloured by chain, top view.
Source organism: Lactobacillus leichmannii
Primary publication:
The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer.
Sintchak MD, Arjara G, Kellogg BA, Stubbe J, Drennan CL
Nat Struct Biol 9 293-300 (2002)
PMID: 11875520

Function and Biology Details

Reaction catalysed: 
2'-deoxyribonucleoside triphosphate + thioredoxin disulfide + H(2)O = ribonucleoside triphosphate + thioredoxin
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176802 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenosylcobalamin-dependent ribonucleoside-triphosphate reductase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 739 amino acids
Theoretical weight: 82.07 KDa
Source organism: Lactobacillus leichmannii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q59490 (Residues: 1-739; Coverage: 100%)
Gene name: rtpR
Sequence domains: Ribonucleotide reductase alpha domain
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21
Unit cell:
a: 120.5Å b: 114.7Å c: 121.3Å
α: 90° β: 110.2° γ: 90°
R-values:
R R work R free
0.234 0.223 0.266
Expression system: Escherichia coli

Quick links

Citations

22 review citations

Ribonucleotide reductases.
Nordlund et al. (2006)
21 more

10 mentions without citation

The origin and evolution of ribonucleotide reduction.
Lundin et al. (2015)
9 more