› 3px2

X-ray diffraction
1.65Å resolution

Structure of TylM1 from Streptomyces fradiae H123N mutant in complex with SAH and dTDP-Quip3N

Released:
DOI: 10.2210/pdb3px2/pdb
PDB entry 3px2 coloured by chain, front view.
PDB entry 3px2 coloured by chain, side view.
PDB entry 3px2 coloured by chain, top view.
Source organism: Streptomyces fradiae
Primary publication:
Molecular architecture of TylM1 from Streptomyces fradiae: an N,N-dimethyltransferase involved in the production of dTDP-D-mycaminose.
Carney AE, Holden HM
Biochemistry 50 780-7 (2011)
PMID: 21142177

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, D
Molecule details ›
Chains: A, D
Length: 262 amino acids
Theoretical weight: 28.38 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 2 x SAH
2 bound ligands:
Ligand T3Q 2 x T3Q
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 86.571Å b: 40.703Å c: 87.208Å
α: 90° β: 117.93° γ: 90°
R-values:
R R work R free
0.197 0.194 0.245
Expression system: Escherichia coli BL21(DE3)

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Citations

4 review citations

Architectures, mechanisms and molecular evolution of natural product methyltransferases.
Liscombe et al. (2012)
3 more