X-ray diffraction
1.6Å resolution

Crystal structure of the tylM1 N,N-dimethyltransferase in complex with SAH and TDP-Qui3NMe2

Source organism: Streptomyces fradiae
Primary publication:
Production of a novel N-monomethylated dideoxysugar.
Biochemistry 53 1105-7 (2014)
PMID: 24512254

Function and Biology Details

Reaction catalysed:
2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose = 2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 263 amino acids
Theoretical weight: 28.54 KDa
Source organism: Streptomyces fradiae
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P95748 (Residues: 1-255; Coverage: 100%)
Gene names: tylM1, tylMI
Sequence domains: Methyltransferase domain
Structure domains:

Ligands and Environments

Cofactor: Ligand SAH 4 x SAH
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P21
Unit cell:
a: 73.532Å b: 92.05Å c: 80.177Å
α: 90° β: 106.1° γ: 90°
R R work R free
0.182 0.181 0.216
Expression system: Escherichia coli BL21(DE3)