› 1y97

X-ray diffraction
2.5Å resolution

The human TREX2 3' exonuclease structure suggests a mechanism for efficient non-processive DNA catalysis

Released:
DOI: 10.2210/pdb1y97/pdb
PDB entry 1y97 coloured by chain, front view.
PDB entry 1y97 coloured by chain, side view.
PDB entry 1y97 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The human TREX2 3' -> 5'-exonuclease structure suggests a mechanism for efficient nonprocessive DNA catalysis.
Perrino FW, Harvey S, McMillin S, Hollis T
J Biol Chem 280 15212-8 (2005)
PMID: 15661738

Function and Biology Details

Reaction catalysed: 
Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189662 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Three prime repair exonuclease 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 238 amino acids
Theoretical weight: 26.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9BQ50 (Residues: 1-236; Coverage: 100%)
Gene name: TREX2
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P212121
Unit cell:
a: 52.5Å b: 77.2Å c: 101.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.205 0.261
Expression system: Escherichia coli

Quick links

Citations

3 review citations

DNA polymerases and human disease.
Loeb et al. (2008)
2 more

10 mentions without citation

Nucleases: diversity of structure, function and mechanism.
Yang W. (2011)
9 more