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TitleStructure-function analyses of isochorismate-pyruvate lyase from Pseudomonas aeruginosa suggest differing catalytic mechanisms for the two pericyclic reactions of this bifunctional enzyme
Journal, issue, pagesBiochemistry, Vol. 48, Page 5239-5245, Year 2009
Publish dateMay 14, 2009 (structure data deposition date)
AuthorsLuo, Q. / Olucha, J. / Lamb, A.L.
External linksBiochemistry / PubMed:19432488
MethodsX-ray diffraction
Resolution2.25 - 2.5 Å
Structure data

PDB-3hgw:
Apo Structure of Pseudomonas aeruginosa Isochorismate-Pyruvate Lyase I87T mutant
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

PDB-3hgx:
Crystal Structure of Pseudomonas aeruginosa Isochorismate-Pyruvate Lyase K42A mutant in complex with salicylate and pyruvate
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SAL:
2-HYDROXYBENZOIC ACID

ChemComp-PYR:
PYRUVIC ACID

Source
  • pseudomonas aeruginosa (bacteria)
KeywordsLYASE / siderophore biosynthesis / pyochelin / isochorismate-pyruvate lyase / chorismate mutase / PchB

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