› 1azo

X-ray diffraction
1.7Å resolution

DNA MISMATCH REPAIR PROTEIN MUTH FROM E. COLI

Released:
DOI: 10.2210/pdb1azo/pdb
PDB entry 1azo coloured by chain, front view.
PDB entry 1azo coloured by chain, side view.
PDB entry 1azo coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural basis for MutH activation in E.coli mismatch repair and relationship of MutH to restriction endonucleases.
Ban C, Yang W
EMBO J 17 1526-34 (1998)
PMID: 9482749

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139160 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA mismatch repair protein MutH Chain: A
Molecule details ›
Chain: A
Length: 232 amino acids
Theoretical weight: 25.85 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P06722 (Residues: 1-229; Coverage: 100%)
Gene names: JW2799, b2831, mutH, mutR, prv
Sequence domains: DNA mismatch repair enzyme MutH
Structure domains: DNA mismatch repair MutH/Restriction endonuclease, type II

Ligands and Environments

1 bound ligand:
Ligand EDO 11 x EDO
1 modified residue:
Ligand MSE 2 x MSE

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 41.6Å b: 72.61Å c: 72.87Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.203 0.263
Expression system: Escherichia coli

Quick links

Citations

25 review citations

DNA mismatch repair.
Kunkel et al. (2005)
24 more

7 mentions without citation

The structural basis of damaged DNA recognition and endonucleolytic cleavage for very short patch repair endonuclease.
Tsutakawa et al. (2001)
6 more