› 1jn3

X-ray diffraction
2.35Å resolution

FIDELITY PROPERTIES AND STRUCTURE OF M282L MUTATOR MUTANT OF DNA POLYMERASE: SUBTLE STRUCTURAL CHANGES INFLUENCE THE MECHANISM OF NUCLEOTIDE DISCRIMINATION

Released:
DOI: 10.2210/pdb1jn3/pdb
PDB entry 1jn3 coloured by chain, front view.
PDB entry 1jn3 coloured by chain, side view.
PDB entry 1jn3 coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
A DNA polymerase beta mutator mutant with reduced nucleotide discrimination and increased protein stability.
Shah AM, Conn DA, Li SX, Capaldi A, Jäger J, Sweasy JB
Biochemistry 40 11372-81 (2001)
PMID: 11560485

Function and Biology Details

Reactions catalysed: 
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139217 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA polymerase beta Chain: A
Molecule details ›
Chain: A
Length: 251 amino acids
Theoretical weight: 29.13 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P06766 (Residues: 85-335; Coverage: 75%)
Gene name: Polb
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21212
Unit cell:
a: 119.54Å b: 63.62Å c: 37.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.215 0.256
Expression system: Escherichia coli

Quick links

Citations

2 review citations

DNA polymerase family X: function, structure, and cellular roles.
Yamtich et al. (2010)
1 more

1 mention without citation

Catalytic effects of mutations of distant protein residues in human DNA polymerase β: theory and experiment.
Klvaňa et al. (2012)