› 1q0t

X-ray diffraction
3.1Å resolution

Ternary Structure of T4DAM with AdoHcy and DNA

Released:
DOI: 10.2210/pdb1q0t/pdb
PDB entry 1q0t coloured by chain, front view.
PDB entry 1q0t coloured by chain, side view.
PDB entry 1q0t coloured by chain, top view.
Source organism: Tequatrovirus T4
Primary publication:
Structure of the bacteriophage T4 DNA adenine methyltransferase.
Yang Z, Horton JR, Zhou L, Zhang XJ, Dong A, Zhang X, Schlagman SL, Kossykh V, Hattman S, Cheng X
Nat Struct Biol 10 849-55 (2003)
PMID: 12937411

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + adenine in DNA = S-adenosyl-L-homocysteine + N-6-methyladenine in DNA
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-114418 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
Macromolecules (2 distinct):
DNA adenine methylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 259 amino acids
Theoretical weight: 30.46 KDa
Source organism: Escherichia virus T4
Expression system: Escherichia coli
UniProt:
  • Canonical: P04392 (Residues: 1-259; Coverage: 100%)
Gene name: DAM
Sequence domains: D12 class N6 adenine-specific DNA methyltransferase
Structure domains:
5'-D(*AP*CP*AP*GP*GP*AP*TP*CP*CP*TP*GP*T)-3' Chains: C, D
Molecule details ›
Chains: C, D
Length: 12 nucleotides
Theoretical weight: 3.66 KDa
Source organism: Tequatrovirus T4
Expression system: Not provided

Ligands and Environments


Cofactor: Ligand SAH 2 x SAH
1 bound ligand:
Ligand IOD 2 x IOD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: P21
Unit cell:
a: 39.7Å b: 109.7Å c: 73.6Å
α: 90° β: 104.2° γ: 90°
R-values:
R R work R free
0.238 0.238 0.293
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

3 review citations

Dam methylation: coordinating cellular processes.
Løbner-Olesen et al. (2005)
2 more

3 mentions without citation

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