› 2h9c

X-ray diffraction
2.35Å resolution

Native Crystal Structure of the Isochorismate-Pyruvate Lyase from Pseudomonas aeruginosa

Released:
DOI: 10.2210/pdb2h9c/pdb
PDB entry 2h9c coloured by chain, front view.
PDB entry 2h9c coloured by chain, side view.
PDB entry 2h9c coloured by chain, top view.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
Two crystal structures of the isochorismate pyruvate lyase from Pseudomonas aeruginosa.
Zaitseva J, Lu J, Olechoski KL, Lamb AL
J Biol Chem 281 33441-9 (2006)
PMID: 16914555

Function and Biology Details

Reactions catalysed: 
Isochorismate = salicylate + pyruvate
Chorismate = prephenate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
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: 99 amino acids
Theoretical weight: 11.3 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q51507 (Residues: 1-99; Coverage: 98%)
Gene names: PA4230, pchB
Sequence domains: Chorismate mutase type II
Structure domains: Chorismate mutase

Ligands and Environments

1 bound ligand:
Ligand NO3 5 x NO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P43212
Unit cell:
a: 93.148Å b: 93.148Å c: 60.19Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.224 0.269
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Protein design by directed evolution.
Jäckel et al. (2008)
5 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