› 5o5c

X-ray diffraction
2.1Å resolution

The crystal structure of DfoJ, the desferrioxamine biosynthetic pathway lysine decarboxylase from the fire blight disease pathogen Erwinia amylovora

Released:
DOI: 10.2210/pdb5o5c/pdb
PDB 5o5c coloured by chain and viewed from the front.
PDB 5o5c coloured by chain and viewed from the side.
PDB 5o5c coloured by chain and viewed from the top.
Source organism: Erwinia amylovora CFBP1430
Primary publication:
A complete structural characterization of the desferrioxamine E biosynthetic pathway from the fire blight pathogen Erwinia amylovora.
Salomone-Stagni M, Bartho JD, Polsinelli I, Bellini D, Walsh MA, Demitri N, Benini S
J. Struct. Biol. (2018)
PMID: 29428557

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative decarboxylase involved in desferrioxamine biosynthesis Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 519 amino acids
Theoretical weight: 56.95 KDa
Source organism: Erwinia amylovora CFBP1430
Expression system: Escherichia coli
UniProt:
  • Canonical: D4I245 (Residues: 1-517; Coverage: 100%)
Gene names: EAMY_3238, dfoJ
Sequence domains: Pyridoxal-dependent decarboxylase conserved domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand PLP 6 x PLP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P32
Unit cell:
a: 269.791Å b: 269.791Å c: 56.194Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.166 0.165 0.187
Expression system: Escherichia coli

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Citations

1 review citation

Flavin-dependent N-hydroxylating enzymes: distribution and application.
Mügge et al. (2020)
6 other articles