› 5xd3

X-ray diffraction
1.78Å resolution

Crystal structure of Mycobacterium smegmatis MutT1 in complex with ATP (I)

Released:
DOI: 10.2210/pdb5xd3/pdb
Model geometry
Fit model/data
PDB entry 5xd3 coloured by chain, front view.
PDB entry 5xd3 coloured by chain, side view.
PDB entry 5xd3 coloured by chain, top view.
Source organism: Mycolicibacterium smegmatis MC2 155
Primary publication:
Hydrolysis of diadenosine polyphosphates. Exploration of an additional role of Mycobacterium smegmatis MutT1.
Arif SM, Varshney U, Vijayan M
J Struct Biol 199 165-176 (2017)
PMID: 28705712

Function and Biology Details

Reactions catalysed: 
8-oxo-GDP + H(2)O = 8-oxo-GMP + phosphate
P(1),P(4)-bis(5'-adenosyl)tetraphosphate + H(2)O = ATP + AMP
8-oxo-GTP + H(2)O = 8-oxo-GDP + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106333 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
8-oxo-(d)GTP phosphatase Chain: A
Molecule details ›
Chain: A
Length: 342 amino acids
Theoretical weight: 38.15 KDa
Source organism: Mycolicibacterium smegmatis MC2 155
Expression system: Escherichia coli
UniProt:
  • Canonical: A0QUZ2 (Residues: 1-322; Coverage: 100%)
Gene names: MSMEG_2390, MSMEI_2330, mutT1
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand ATP 2 x ATP
Ligand GOL 1 x GOL
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P21
Unit cell:
a: 42.03Å b: 84.21Å c: 43.79Å
α: 90° β: 92.89° γ: 90°
R-values:
R R work R free
0.164 0.162 0.204
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

1 mention without citation

Multiple substrate recognition by yeast diadenosine and diphosphoinositol polyphosphate phosphohydrolase through phosphate clamping.
Márquez-Moñino et al. (2021)