› 4oqd

X-ray diffraction
1.6Å resolution

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

Released:
DOI: 10.2210/pdb4oqd/pdb
PDB entry 4oqd coloured by chain, front view.
PDB entry 4oqd coloured by chain, side view.
PDB entry 4oqd coloured by chain, top view.
Source organism: Streptomyces fradiae
Primary publication:
Production of a novel N-monomethylated dideoxysugar.
Thoden JB, Holden HM
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
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161176 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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)
UniProt:
  • 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:
Ligand QDM 4 x QDM
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-values:
R R work R free
0.182 0.181 0.216
Expression system: Escherichia coli BL21(DE3)

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Citations

2 citation in other articles

Molecular architecture of KedS8, a sugar N-methyltransferase from Streptoalloteichus sp. ATCC 53650.
Delvaux et al. (2015)
1 more

1 mention without citation

Production of a novel N-monomethylated dideoxysugar.
Thoden et al. (2014)