› 2bsy

X-ray diffraction
1.5Å resolution

Epstein Barr Virus dUTPase

Released:
DOI: 10.2210/pdb2bsy/pdb
PDB entry 2bsy coloured by chain, front view.
PDB entry 2bsy coloured by chain, side view.
PDB entry 2bsy coloured by chain, top view.
Source organism: Human gammaherpesvirus 4
Primary publication:
The monomeric dUTPase from Epstein-Barr virus mimics trimeric dUTPases.
Tarbouriech N, Buisson M, Seigneurin JM, Cusack S, Burmeister WP
Structure 13 1299-310 (2005)
PMID: 16154087

Function and Biology Details

Reaction catalysed: 
dUTP + H(2)O = dUMP + diphosphate
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-136646 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Deoxyuridine 5'-triphosphate nucleotidohydrolase Chain: A
Molecule details ›
Chain: A
Length: 278 amino acids
Theoretical weight: 30.99 KDa
Source organism: Human gammaherpesvirus 4
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P03195 (Residues: 1-278; Coverage: 100%)
Gene names: BLLF3, DUT
Sequence domains: dUTPase
Structure domains: Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A

Ligands and Environments

2 bound ligands:
Ligand UMP 1 x UMP
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 56.655Å b: 55.787Å c: 81.053Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.15 0.148 0.187
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

Viral proteomics.
Maxwell et al. (2007)
6 more

2 mentions without citation

The flexible motif V of Epstein-Barr virus deoxyuridine 5'-triphosphate pyrophosphatase is essential for catalysis.
Freeman et al. (2009)
1 more