› 2noi

X-ray diffraction
2.35Å resolution

Structure of G42A human 8-oxoguanine glycosylase crosslinked to undamaged G-containing DNA

Released:
DOI: 10.2210/pdb2noi/pdb
PDB entry 2noi coloured by chain, front view.
PDB entry 2noi coloured by chain, side view.
PDB entry 2noi coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural characterization of human 8-oxoguanine DNA glycosylase variants bearing active site mutations.
Radom CT, Banerjee A, Verdine GL
J Biol Chem 282 9182-94 (2007)
PMID: 17114185

Function and Biology Details

Reaction catalysed: 
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:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-115672 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
N-glycosylase/DNA lyase Chain: A
Molecule details ›
Chain: A
Length: 325 amino acids
Theoretical weight: 36.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O15527 (Residues: 12-327; Coverage: 92%)
Gene names: MMH, MUTM, OGG1, OGH1
Sequence domains:
Structure domains:
5'-D(*GP*GP*TP*AP*GP*AP*CP*CP*TP*GP*GP*AP*CP*GP*C)-3' Chain: B
Molecule details ›
Chain: B
Length: 15 nucleotides
Theoretical weight: 4.64 KDa
Source organism: Homo sapiens
Expression system: Not provided
5'-D(*GP*CP*GP*TP*C*CP*AP*GP*GP*TP*CP*TP*AP*CP*C)-3' Chain: C
Molecule details ›
Chain: C
Length: 15 nucleotides
Theoretical weight: 4.55 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P6522
Unit cell:
a: 91.888Å b: 91.888Å c: 211.835Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.226 0.226 0.259
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

8 review citations

Base excision repair.
Krokan et al. (2013)
7 more

3 mentions without citation

Recent advances in the structural mechanisms of DNA glycosylases.
Brooks et al. (2013)
2 more