› 3hgx

X-ray diffraction
2.5Å resolution

Crystal Structure of Pseudomonas aeruginosa Isochorismate-Pyruvate Lyase K42A mutant in complex with salicylate and pyruvate

Released:
DOI: 10.2210/pdb3hgx/pdb
PDB entry 3hgx coloured by chain, front view.
PDB entry 3hgx coloured by chain, side view.
PDB entry 3hgx 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
Molecule details ›
Chains: A, B
Length: 101 amino acids
Theoretical weight: 11.39 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

2 bound ligands:
Ligand SAL 2 x SAL
Ligand PYR 2 x PYR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P212121
Unit cell:
a: 48.015Å b: 53.15Å c: 82.336Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.216 0.276
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

2 mentions without citation

Modification of residue 42 of the active site loop with a lysine-mimetic side chain rescues isochorismate-pyruvate lyase activity in Pseudomonas aeruginosa PchB.
Olucha et al. (2012)
1 more