› 5je4

X-ray diffraction
1.93Å resolution

Crystal structure of Burkholderia glumae ToxA Y7A mutant with bound S-adenosylhomocysteine (SAH)

Released:
DOI: 10.2210/pdb5je4/pdb
PDB entry 5je4 coloured by chain, front view.
PDB entry 5je4 coloured by chain, side view.
PDB entry 5je4 coloured by chain, top view.
Source organism: Burkholderia glumae
Primary publication:
Burkholderia glumae ToxA Is a Dual-Specificity Methyltransferase That Catalyzes the Last Two Steps of Toxoflavin Biosynthesis.
Fenwick MK, Philmus B, Begley TP, Ealick SE
Biochemistry 55 2748-59 (2016)
PMID: 27070241

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192242 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methyltransferase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 247 amino acids
Theoretical weight: 27.73 KDa
Source organism: Burkholderia glumae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9LBJ0 (Residues: 1-245; Coverage: 100%)
Gene names: CEQ24_001050, toxA
Sequence domains: Methyltransferase domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P212121
Unit cell:
a: 46.515Å b: 66.622Å c: 145.056Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.168 0.227
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Heteroatom-Heteroatom Bond Formation in Natural Product Biosynthesis.
Waldman et al. (2017)
2 more

1 mention without citation

Burkholderia glumae ToxA Is a Dual-Specificity Methyltransferase That Catalyzes the Last Two Steps of Toxoflavin Biosynthesis.
Fenwick et al. (2016)