› 2a1s

X-ray diffraction
2.6Å resolution

Crystal structure of native PARN nuclease domain

Released:
DOI: 10.2210/pdb2a1s/pdb
PDB entry 2a1s coloured by chain, front view.
PDB entry 2a1s coloured by chain, side view.
PDB entry 2a1s coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural insight into poly(A) binding and catalytic mechanism of human PARN.
Wu M, Reuter M, Lilie H, Liu Y, Wahle E, Song H
EMBO J 24 4082-93 (2005)
PMID: 16281054

Function and Biology Details

Reaction catalysed: 
Exonucleolytic cleavage of poly(A) to 5'-AMP
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131934 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Poly(A)-specific ribonuclease PARN Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 430 amino acids
Theoretical weight: 49.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O95453 (Residues: 1-430; Coverage: 67%)
Gene names: DAN, PARN
Sequence domains: CAF1 family ribonuclease
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2
Unit cell:
a: 205.54Å b: 123.016Å c: 82.844Å
α: 90° β: 112.59° γ: 90°
R-values:
R R work R free
0.243 0.219 0.254
Expression system: Escherichia coli

Quick links

Citations

15 review citations

Multifunctional deadenylase complexes diversify mRNA control.
Goldstrohm et al. (2008)
14 more

11 mentions without citation

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