› 1svu

X-ray diffraction
2.66Å resolution

Structure of the Q237W mutant of HhaI DNA methyltransferase: an insight into protein-protein interactions

Released:
DOI: 10.2210/pdb1svu/pdb
PDB entry 1svu coloured by chain, front view.
PDB entry 1svu coloured by chain, side view.
PDB entry 1svu coloured by chain, top view.
Source organism: Haemophilus haemolyticus
Primary publication:
Structure of the Q237W mutant of HhaI DNA methyltransferase: an insight into protein-protein interactions.
Dong A, Zhou L, Zhang X, Stickel S, Roberts RJ, Cheng X
Biol Chem 385 373-9 (2004)
PMID: 15195996

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
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-138430 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Type II methyltransferase M.HhaI Chains: A, B
Molecule details ›
Chains: A, B
Length: 327 amino acids
Theoretical weight: 37.1 KDa
Source organism: Haemophilus haemolyticus
Expression system: Escherichia coli
UniProt:
  • Canonical: P05102 (Residues: 1-327; Coverage: 100%)
Gene name: hhaIM
Sequence domains: C-5 cytosine-specific DNA methylase
Structure domains:

Ligands and Environments


Cofactor: Ligand SAH 2 x SAH
2 bound ligands:
Ligand SO4 2 x SO4
Ligand UNX 17 x UNX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: C2
Unit cell:
a: 155Å b: 47Å c: 122.7Å
α: 90° β: 121° γ: 90°
R-values:
R R work R free
0.189 0.189 0.266
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Structure, function and mechanism of exocyclic DNA methyltransferases.
Bheemanaik et al. (2006)
3 more

2 mentions without citation

Structure of the Q237W mutant of HhaI DNA methyltransferase: an insight into protein-protein interactions.
Dong et al. (2004)
1 more