› 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 entry 5o5c coloured by chain, front view.
PDB entry 5o5c coloured by chain, side view.
PDB entry 5o5c coloured by chain, top view.
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 202 236-249 (2018)
PMID: 29428557

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112637 (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)
9 other articles