› 1ci7

X-ray diffraction
2.6Å resolution

TERNARY COMPLEX OF THYMIDYLATE SYNTHASE FROM PNEUMOCYSTIS CARINII

Released:
DOI: 10.2210/pdb1ci7/pdb
PDB entry 1ci7 coloured by chain, front view.
PDB entry 1ci7 coloured by chain, side view.
PDB entry 1ci7 coloured by chain, top view.
Source organism: Pneumocystis carinii
Primary publication:
The structural mechanism for half-the-sites reactivity in an enzyme, thymidylate synthase, involves a relay of changes between subunits.
Anderson AC, O'Neil RH, DeLano WL, Stroud RM
Biochemistry 38 13829-36 (1999)
PMID: 10529228

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-146467 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 297 amino acids
Theoretical weight: 34.4 KDa
Source organism: Pneumocystis carinii
Expression system: Escherichia coli
UniProt:
  • Canonical: P13100 (Residues: 1-297; Coverage: 100%)
Gene name: THYA
Sequence domains: Thymidylate synthase
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain

Ligands and Environments

2 bound ligands:
Ligand UMP 2 x UMP
Ligand CB3 1 x CB3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P212121
Unit cell:
a: 66.16Å b: 178.76Å c: 54.05Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.221 0.294
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Thermodynamic and NMR Assessment of Ligand Cooperativity and Intersubunit Communication in Symmetric Dimers: Application to Thymidylate Synthase.
Lee et al. (2018)
37 other articles

2 mentions without citation

Structures of human thymidylate synthase R163K with dUMP, FdUMP and glutathione show asymmetric ligand binding.
Gibson et al. (2011)
1 more