› 3hgw

X-ray diffraction
2.25Å resolution

Apo Structure of Pseudomonas aeruginosa Isochorismate-Pyruvate Lyase I87T mutant

Released:
DOI: 10.2210/pdb3hgw/pdb
PDB entry 3hgw coloured by chain, front view.
PDB entry 3hgw coloured by chain, side view.
PDB entry 3hgw coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Structure-function analyses of isochorismate-pyruvate lyase from Pseudomonas aeruginosa suggest differing catalytic mechanisms for the two pericyclic reactions of this bifunctional enzyme.
Luo Q, Olucha J, Lamb AL
Biochemistry 48 5239-45 (2009)
PMID: 19432488

Function and Biology Details

Reactions catalysed: 
Isochorismate = salicylate + pyruvate
Chorismate = prephenate
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-175949 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isochorismate pyruvate lyase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 101 amino acids
Theoretical weight: 11.44 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: Q51507 (Residues: 1-101; Coverage: 100%)
Gene names: PA4230, pchB
Sequence domains: Chorismate mutase type II
Structure domains: Chorismate mutase

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P212121
Unit cell:
a: 54.503Å b: 74.919Å c: 88.505Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.219 0.256
Expression system: Escherichia coli

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Citations

3 review citations

Nonribosomal peptides for iron acquisition: pyochelin biosynthesis as a case study.
Ronnebaum et al. (2018)
2 more