Gotthard Guillaume, Hiblot Julien, Elias Mikael, Chabrière Eric
Architecture et Fonction des Macromolécules Biologiques, CNRS-Aix Marseille Université, 13288 Marseille, France.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Mar 1;67(Pt 3):354-7. doi: 10.1107/S1744309110053819. Epub 2011 Feb 25.
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 (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.
磷酸三酯酶样内酯酶（PLLs）是一类有趣的酶家族，就其催化功能而言，它们在生物技术领域具有至关重要的意义。作为天然内酯酶，它们可能通过关闭群体感应系统（群体猝灭）来对抗诸如铜绿假单胞菌等病原体，从而降低病原体的毒力。由于其具有广泛的磷酸三酯酶活性，能够使诸如农药和神经毒剂等有毒有机磷化合物失活，它们作为有效的生物清除剂同样具有吸引力。已鉴定出PLL家族的一个新成员（SisPox），并从嗜热古菌冰岛硫化叶菌中克隆了其基因。由于其超耐热结构，SisPox似乎是工程研究的一个良好候选对象。本文报道了这种来自嗜热冰岛硫化叶菌的内酯酶的生产、纯化、结晶条件以及分辨率为2.34 Å的数据收集情况。
