› 1ewn

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF THE HUMAN AAG DNA REPAIR GLYCOSYLASE COMPLEXED WITH 1,N6-ETHENOADENINE-DNA

Released:
DOI: 10.2210/pdb1ewn/pdb
PDB entry 1ewn coloured by chain, front view.
PDB entry 1ewn coloured by chain, side view.
PDB entry 1ewn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG.
Lau AY, Wyatt MD, Glassner BJ, Samson LD, Ellenberger T
Proc Natl Acad Sci U S A 97 13573-8 (2000)
PMID: 11106395

Function and Biology Details

Reaction catalysed: 
Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine and 7-methyladenine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-113774 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
DNA-3-methyladenine glycosylase Chain: A
Molecule details ›
Chain: A
Length: 219 amino acids
Theoretical weight: 24.33 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P29372 (Residues: 80-298; Coverage: 74%)
Gene names: AAG, ANPG, MID1, MPG
Sequence domains: Methylpurine-DNA glycosylase (MPG)
Structure domains: Methylpurine-DNA glycosylase (MPG)
DNA (5'-D(*GP*AP*CP*AP*TP*GP*(EDA)P*TP*TP*GP*CP*C)-3') Chain: D
Molecule details ›
Chain: D
Length: 12 nucleotides
Theoretical weight: 3.69 KDa
Source organism: Homo sapiens
Expression system: Not provided
DNA (5'-D(P*GP*CP*AP*AP*TP*CP*AP*TP*GP*TP*CP*A)-3') Chain: E
Molecule details ›
Chain: E
Length: 12 nucleotides
Theoretical weight: 3.65 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand NA 1 x NA
1 modified residue:
Ligand EDA 1 x EDA

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 42.145Å b: 57.336Å c: 125.517Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.23 0.259
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

30 review citations

Genome editing with CRISPR-Cas nucleases, base editors, transposases and prime editors.
Anzalone et al. (2020)
29 more

22 mentions without citation

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