Open AccessCrystallization and preliminary X‐ray diffraction analysis of the hyperthermophilic Sulfolobus islandicus lactonase
Author(s) -
Gotthard Guillaume,
Hiblot Julien,
Elias Mikael,
Chabrière Eric
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110053819
Subject(s) - quorum quenching , sulfolobus , quorum sensing , biology , virulence , pseudomonas aeruginosa , archaea , microbiology and biotechnology , hyperthermophile , genetics , gene , bacteria
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 organophosphorus compounds such as pesticides and nerve agents, they are equally appealing as potent bioscavengers. A new representative of the PLL family has been identified ( Sis Pox) and its gene was cloned from the hyperthermophilic archeon Sulfolobus islandicus . Owing to its hyperthermostable architecture, Sis Pox 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 .