› 1sjn

X-ray diffraction
1.8Å resolution

Mycobacterium tuberculosis dUTPase complexed with magnesium and alpha,beta-imido-dUTP

Released:
DOI: 10.2210/pdb1sjn/pdb
PDB entry 1sjn coloured by chain, front view.
PDB entry 1sjn coloured by chain, side view.
PDB entry 1sjn coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Crystal structure of the Mycobacterium tuberculosis dUTPase: insights into the catalytic mechanism.
Chan S, Segelke B, Lekin T, Krupka H, Cho US, Kim MY, So M, Kim CY, Naranjo CM, Rogers YC, Park MS, Waldo GS, Pashkov I, Cascio D, Perry JL, Sawaya MR
J Mol Biol 341 503-17 (2004)
PMID: 15276840

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:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161882 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Deoxyuridine 5'-triphosphate nucleotidohydrolase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 170 amino acids
Theoretical weight: 17.57 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WNS5 (Residues: 1-154; Coverage: 100%)
Gene names: MTCY05A6.18c, Rv2697c, dut
Sequence domains: dUTPase
Structure domains: Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A

Ligands and Environments

4 bound ligands:
Ligand MG 3 x MG
Ligand DUP 3 x DUP
Ligand TRS 1 x TRS
Ligand NO3 2 x NO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P212121
Unit cell:
a: 57.521Å b: 78.506Å c: 94.509Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.168 0.198
Expression system: Escherichia coli

Quick links

Citations

6 review citations

The phage-related chromosomal islands of Gram-positive bacteria.
Novick et al. (2010)
5 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