› 2oa8

X-ray diffraction
2.1Å resolution

Crystal Structure of mTREX1 with ssDNA

Released:
DOI: 10.2210/pdb2oa8/pdb
PDB entry 2oa8 coloured by chain, front view.
PDB entry 2oa8 coloured by chain, side view.
PDB entry 2oa8 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
The crystal structure of TREX1 explains the 3' nucleotide specificity and reveals a polyproline II helix for protein partnering.
de Silva U, Choudhury S, Bailey SL, Harvey S, Perrino FW, Hollis T
J Biol Chem 282 10537-43 (2007)
PMID: 17293595

Function and Biology Details

Reaction catalysed: 
Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-115725 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
Macromolecules (2 distinct):
Three-prime repair exonuclease 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 233 amino acids
Theoretical weight: 25.58 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q91XB0 (Residues: 5-234; Coverage: 73%)
Gene name: Trex1
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H
5'-D(*GP*AP*CP*G)-3' Chains: C, D
Molecule details ›
Chains: C, D
Length: 4 nucleotides
Theoretical weight: 1.22 KDa
Source organism: Mus musculus
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand CA 4 x CA
1 modified residue:
Ligand MSE 4 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 64.85Å b: 57.141Å c: 68.47Å
α: 90° β: 107.47° γ: 90°
R-values:
R R work R free
0.195 0.192 0.259
Expression systems:
  • Escherichia coli BL21
  • Not provided

Quick links

Citations

8 review citations

Polyproline-II helix in proteins: structure and function.
Adzhubei et al. (2013)
7 more

13 mentions without citation

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