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

Guillaume Gotthard, Julien Hiblot, Daniel Gonzalez, Eric Chabrière, Mikael Elias

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

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 organo phosphorus 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.

Original languageEnglish (US)
Pages (from-to)73-76
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume69
Issue number1
DOIs
StatePublished - Jan 2013

Keywords

  • Pseudomonas pseudoalcaligenes
  • lactonases
  • nerve agents
  • organophosphorus
  • pesticides
  • phosphotriesterases
  • quorum quenching
  • quorum sensing

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