› 2a9w

X-ray diffraction
1.65Å resolution

E. coli TS complexed with dUMP and inhibitor GA9

Released:
DOI: 10.2210/pdb2a9w/pdb
PDB entry 2a9w coloured by chain, front view.
PDB entry 2a9w coloured by chain, side view.
PDB entry 2a9w coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The structure of Cryptococcus neoformans thymidylate synthase suggests strategies for using target dynamics for species-specific inhibition.
Finer-Moore JS, Anderson AC, O'Neil RH, Costi MP, Ferrari S, Krucinski J, Stroud RM
Acta Crystallogr D Biol Crystallogr 61 1320-34 (2005)
PMID: 16204883

Function and Biology Details

Reaction catalysed: 
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
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-141681 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 264 amino acids
Theoretical weight: 30.56 KDa
Source organism: Escherichia coli
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

6 bound ligands:
Ligand PO4 12 x PO4
Ligand UMP 4 x UMP
Ligand GA9 4 x GA9
Ligand BME 4 x BME
Ligand GOL 10 x GOL
Ligand 2BR 1 x 2BR
1 modified residue:
Ligand CXM 4 x CXM

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: R3
Unit cell:
a: 186.6Å b: 186.6Å c: 114.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.207 0.226
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

In vivo mutations of thymidylate synthase (encoded by thyA) are responsible for thymidine dependency in clinical small-colony variants of Staphylococcus aureus.
Chatterjee et al. (2008)
2 more