› 4epp

X-ray diffraction
1.95Å resolution

Canonical poly(ADP-ribose) glycohydrolase from Tetrahymena thermophila.

Released:
DOI: 10.2210/pdb4epp/pdb
PDB entry 4epp coloured by chain, front view.
PDB entry 4epp coloured by chain, side view.
PDB entry 4epp coloured by chain, top view.
Source organism: Tetrahymena thermophila
Primary publication:
Structure and mechanism of a canonical poly(ADP-ribose) glycohydrolase.
Dunstan MS, Barkauskaite E, Lafite P, Knezevic CE, Brassington A, Ahel M, Hergenrother PJ, Leys D, Ahel I
Nat Commun 3 878 (2012)
PMID: 22673905

Function and Biology Details

Reaction catalysed: 
Hydrolyzes poly(ADP-D-ribose) at glycosidic (1''-2') linkage of ribose-ribose bond to produce free ADP-D-ribose
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125126 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
poly(ADP-ribose) glycohydrolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 477 amino acids
Theoretical weight: 55.89 KDa
Source organism: Tetrahymena thermophila
Expression system: Escherichia coli
UniProt:
  • Canonical: I6L8L8 (Residues: 1-457; Coverage: 100%)
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand APR 2 x APR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P41
Unit cell:
a: 112.7Å b: 112.7Å c: 88.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.167 0.207
Expression system: Escherichia coli

Quick links

Citations

26 review citations

PARP and PARG inhibitors in cancer treatment.
Slade D. (2020)
25 more

6 mentions without citation

Structural biology of the writers, readers, and erasers in mono- and poly(ADP-ribose) mediated signaling.
Karlberg et al. (2013)
5 more