› 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 5je4 coloured by chain and viewed from the front.
PDB 5je4 coloured by chain and viewed from the side.
PDB 5je4 coloured by chain and viewed from the top.
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 (2016)
PMID: 27070241

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (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

2 review citations

A genomics perspective on natural product biosynthesis in plant pathogenic bacteria.
Baldeweg et al. (2019)
1 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)