› 4wpk

X-ray diffraction
0.98Å resolution

Crystal structure of Mycobacterium tuberculosis uracil-DNA glycosylase, Form I

Released:
DOI: 10.2210/pdb4wpk/pdb
PDB entry 4wpk coloured by chain, front view.
PDB entry 4wpk coloured by chain, side view.
PDB entry 4wpk coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Structural plasticity in Mycobacterium tuberculosis uracil-DNA glycosylase (MtUng) and its functional implications.
Arif SM, Geethanandan K, Mishra P, Surolia A, Varshney U, Vijayan M
Acta Crystallogr D Biol Crystallogr 71 1514-27 (2015)
PMID: 26143923

Function and Biology Details

Reaction catalysed: 
Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161423 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uracil-DNA glycosylase Chain: A
Molecule details ›
Chain: A
Length: 238 amino acids
Theoretical weight: 25.81 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WFQ9 (Residues: 1-227; Coverage: 100%)
Gene names: MTCY349.11, Rv2976c, ung
Sequence domains: Uracil DNA glycosylase superfamily
Structure domains: Uracil-DNA glycosylase-like domain

Ligands and Environments

2 bound ligands:
Ligand CIT 1 x CIT
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P21
Unit cell:
a: 38.919Å b: 63.473Å c: 45.186Å
α: 90° β: 112.89° γ: 90°
R-values:
R R work R free
0.137 0.137 0.154
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Guardians of the mycobacterial genome: A review on DNA repair systems in Mycobacterium tuberculosis.
Singh A. (2017)
4 other articles

1 mention without citation

The oxygen-oxygen distance of water in crystallographic data sets.
Palese LL. (2020)