› 1ngn

X-ray diffraction
2.1Å resolution

Mismatch repair in methylated DNA. Structure of the mismatch-specific thymine glycosylase domain of methyl-CpG-binding protein MBD4

Released:
DOI: 10.2210/pdb1ngn/pdb
PDB entry 1ngn coloured by chain, front view.
PDB entry 1ngn coloured by chain, side view.
PDB entry 1ngn coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Mismatch repair in methylated DNA. Structure and activity of the mismatch-specific thymine glycosylase domain of methyl-CpG-binding protein MBD4.
Wu P, Qiu C, Sohail A, Zhang X, Bhagwat AS, Cheng X
J Biol Chem 278 5285-91 (2003)
PMID: 12456671

Function and Biology Details

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-195554 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methyl-CpG-binding domain protein 4 Chain: A
Molecule details ›
Chain: A
Length: 155 amino acids
Theoretical weight: 18.57 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Z2D7 (Residues: 400-554; Coverage: 28%)
Gene name: Mbd4
Structure domains: Hypothetical protein; domain 2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300, NSLS BEAMLINE X12C, NSLS BEAMLINE X26C
Spacegroup: P3121
Unit cell:
a: 48.58Å b: 48.58Å c: 146.57Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.213 0.213 0.263
Expression system: Escherichia coli

Quick links

Citations

14 review citations

DNA base damage recognition and removal: new twists and grooves.
Huffman et al. (2005)
13 more

8 mentions without citation

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