› 1o25

X-ray diffraction
2.4Å resolution

Crystal structure of Thymidylate Synthase Complementing Protein (TM0449) from Thermotoga maritima with dUMP at 2.4 A resolution

Released:
DOI: 10.2210/pdb1o25/pdb
PDB entry 1o25 coloured by chain, front view.
PDB entry 1o25 coloured by chain, side view.
PDB entry 1o25 coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Functional analysis of substrate and cofactor complex structures of a thymidylate synthase-complementing protein.
Mathews II, Deacon AM, Canaves JM, McMullan D, Lesley SA, Agarwalla S, Kuhn P
Structure 11 677-90 (2003)
PMID: 12791256

Function and Biology Details

Reaction catalysed: 
5,10-methylenetetrahydrofolate + dUMP + NADPH = dTMP + tetrahydrofolate + NADP(+)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194544 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Flavin-dependent thymidylate synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 232 amino acids
Theoretical weight: 27.5 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WYT0 (Residues: 1-220; Coverage: 100%)
Gene names: TM_0449, thy1, thyX
Sequence domains: Thymidylate synthase complementing protein
Structure domains: Gyrase A; domain 2

Ligands and Environments

1 bound ligand:
Ligand UMP 4 x UMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P212121
Unit cell:
a: 54.682Å b: 116.703Å c: 141.727Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.198 0.263
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Evolution of protein fold in the presence of functional constraints.
Andreeva et al. (2006)
7 more