› 2vf0

X-ray diffraction
3Å resolution

CRYSTAL STRUCTURE OF THE THYMIDYLATE SYNTHASE K48Q COMPLEXED WITH 5NO2DUMP AND BW1843U89

Released:
DOI: 10.2210/pdb2vf0/pdb
PDB entry 2vf0 coloured by chain, front view.
PDB entry 2vf0 coloured by chain, side view.
PDB entry 2vf0 coloured by chain, top view.
Source organism: Escherichia coli BL21
Primary publication:
Role of an invariant lysine residue in folate binding on Escherichia coli thymidylate synthase: calorimetric and crystallographic analysis of the K48Q mutant.
Arvizu-Flores AA, Sugich-Miranda R, Arreola R, Garcia-Orozco KD, Velazquez-Contreras EF, Montfort WR, Maley F, Sotelo-Mundo RR
Int J Biochem Cell Biol 40 2206-17 (2008)
PMID: 18403248

Function and Biology Details

Reaction catalysed: 
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141681 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 264 amino acids
Theoretical weight: 30.56 KDa
Source organism: Escherichia coli BL21
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A884 (Residues: 1-264; Coverage: 100%)
Gene names: JW2795, b2827, thyA
Sequence domains: Thymidylate synthase
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain

Ligands and Environments

3 bound ligands:
Ligand NDU 2 x NDU
Ligand F89 2 x F89
Ligand SO4 1 x SO4
1 modified residue:
Ligand CXM 2 x CXM

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P63
Unit cell:
a: 127.16Å b: 127.16Å c: 67.95Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.18 0.239
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Survey of the year 2008: applications of isothermal titration calorimetry.
Falconer et al. (2010)
1 more

1 mention without citation

Role of an invariant lysine residue in folate binding on Escherichia coli thymidylate synthase: calorimetric and crystallographic analysis of the K48Q mutant.
Arvizu-Flores et al. (2008)