› 1fxx

X-ray diffraction
2.4Å resolution

THE STRUCTURE OF EXONUCLEASE I SUGGESTS HOW PROCESSIVITY IS ACHIEVED

Released:
DOI: 10.2210/pdb1fxx/pdb
PDB entry 1fxx coloured by chain, front view.
PDB entry 1fxx coloured by chain, side view.
PDB entry 1fxx coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure of Escherichia coli exonuclease I suggests how processivity is achieved.
Breyer WA, Matthews BW
Nat Struct Biol 7 1125-8 (2000)
PMID: 11101894

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:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138310 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Exodeoxyribonuclease I Chain: A
Molecule details ›
Chain: A
Length: 482 amino acids
Theoretical weight: 55.51 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P04995 (Residues: 1-475; Coverage: 100%)
Gene names: JW1993, b2011, cpeA, sbcB, xonA
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 1 x MG
Ligand PO4 1 x PO4
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P6522
Unit cell:
a: 84.41Å b: 84.41Å c: 298.65Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.22 0.204 0.236
Expression system: Escherichia coli

Quick links

Citations

5 review citations

A structural basis for processivity.
Breyer et al. (2001)
4 more

14 mentions without citation

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