Crystallization and preliminary X-ray diffraction analysis of the hyperthermophilic Sulfolobus islandicus lactonase

Guillaume Gotthard, Julien Hiblot, Mikael Elias, Eric Chabrire

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

Phosphotriesterase-like lactonases (PLLs) constitute an interesting family of enzymes that are of paramount interest in biotechnology with respect to their catalytic functions. As natural lactonases, they may act against pathogens such as Pseudomonas aeruginosa by shutting down their quorum-sensing system (quorum quenching) and thus decreasing pathogen virulence. Owing to their promiscuous phosphotriesterase activity, which can inactivate toxic organophos-phorus compounds such as pesticides and nerve agents, they are equally appealing as potent bioscavengers. A new representative of the PLL family has been identified (SisPox) and its gene was cloned from the hyperthermophilic archeon Sulfolobus islandicus. Owing to its hyperthermostable architecture, SisPox appears to be a good candidate for engineering studies. Here, production, purification, crystallization conditions and data collection to 2.34 Å resolution are reported for this lactonase from the hyperthermophilic S. islandicus.

Original languageEnglish (US)
Pages (from-to)354-357
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume67
Issue number3
DOIs
StatePublished - Mar 1 2011

Keywords

  • bioscavengers
  • hyperthermophiles
  • lactonases
  • phosphotriesterase-like lactonases
  • phosphotriesterases
  • quorum quenching
  • quorum sensing

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