› 7ef9

X-ray diffraction
1.97Å resolution

Crystal structure of mouse MUTYH in complex with DNA containing AP site analogue:8-oxoG (Form II)

Released:
DOI: 10.2210/pdb7ef9/pdb
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PDB entry 7ef9 coloured by chain, front view.
PDB entry 7ef9 coloured by chain, side view.
PDB entry 7ef9 coloured by chain, top view.
Source organisms:
Primary publication:
Structure of the mammalian adenine DNA glycosylase MUTYH: insights into the base excision repair pathway and cancer.
Nakamura T, Okabe K, Hirayama S, Chirifu M, Ikemizu S, Morioka H, Nakabeppu Y, Yamagata Y
OpenAccess logo Nucleic Acids Res 49 7154-7163 (2021)
PMID: 34142156

Function and Biology Details

Reaction catalysed: 
Hydrolyzes free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-121249 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
Adenine DNA glycosylase Chain: A
Molecule details ›
Chain: A
Length: 448 amino acids
Theoretical weight: 50.11 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99P21 (Residues: 45-487; Coverage: 86%)
Gene names: Mutyh, Myh
Sequence domains:
DNA (5'-D(*AP*TP*GP*AP*GP*AP*CP*(8OG)P*GP*GP*GP*AP*CP*T)-3') Chain: B
Molecule details ›
Chain: B
Length: 14 nucleotides
Theoretical weight: 4.39 KDa
Source organism: Homo sapiens
Expression system: Not provided
DNA (5'-D(*TP*AP*GP*TP*CP*CP*CP*(3DR)P*GP*TP*CP*TP*C)-3') Chain: C

Ligands and Environments

4 bound ligands:
Ligand SF4 1 x SF4
Ligand ZN 1 x ZN
Ligand SO4 6 x SO4
Ligand GOL 1 x GOL
1 modified residue:
Ligand 8OG 1 x 8OG

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: I222
Unit cell:
a: 71.66Å b: 108.496Å c: 158.527Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.178 0.197
Expression systems:
  • Escherichia coli
  • Not provided

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Citations

2 review citations

From Processivity to Genome Maintenance: The Many Roles of Sliding Clamps.
Mulye et al. (2022)
1 more

1 mention without citation

Structure of the mammalian adenine DNA glycosylase MUTYH: insights into the base excision repair pathway and cancer.
Nakamura et al. (2021)

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