Crystallization and preliminary X-ray diffraction analysis of the organophosphorus hydrolase OPHC2 from Pseudomonas pseudoalcaligenes

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jan 1;69(Pt 1):73-6. doi: 10.1107/S174430911205049X. Epub 2012 Dec 25.


Enzymes that are capable of degrading neurotoxic organophosphorus compounds are of increasing interest because of the lack of efficient and clean methods for their removal. Recently, a novel organophosphorus hydrolase belonging to the metallo-β-lactamase superfamily was identified and isolated from the mesophilic bacterium Pseudomonas pseudoalcaligenes. This enzyme, named OPHC2, is endowed with significant thermal and pH stability, making it an appealing candidate for engineering studies to develop an efficient organophosphorus biodecontaminant. Combined with biochemical studies, structural information will help decipher the catalytic mechanism of organophosphorus hydrolysis by OPHC2 and identify the residues involved in its substrate specificity. Here, the expression, purification, crystallization and X-ray data collection at 2.1 Å resolution of OPHC2 are presented.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aryldialkylphosphatase / chemistry*
  • Aryldialkylphosphatase / genetics
  • Aryldialkylphosphatase / isolation & purification*
  • Aryldialkylphosphatase / metabolism
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification
  • Cloning, Molecular
  • Crystallization / methods
  • Crystallography, X-Ray
  • Kinetics
  • Protein Conformation
  • Pseudomonas pseudoalcaligenes / enzymology


  • Bacterial Proteins
  • Aryldialkylphosphatase