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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Nov;69(Pt 11):1235-8. doi: 10.1107/S1744309113024846. Epub 2013 Oct 17.

Crystallization and preliminary X-ray diffraction analysis of the lactonase VmoLac from Vulcanisaeta moutnovskia.

Author information

1
Unité de Recherche sur les Maladies Infectieuses et Tropicales Emergents (URMITE), UMR CNRS-IRD-INSERM, IHU Méditerranée Infection, Aix-Marseille Université, 7 Boulevard Jean Moulin, 13385 Marseille CEDEX 05, France.

Abstract

Phosphotriesterase-like lactonases (PLLs) are native lactonases that are capable of hydrolyzing lactones such as aliphatic lactones or acyl-homoserine lactones, which are involved in bacterial quorum sensing. Previously characterized PLLs are moreover endowed with a promiscuous phosphotriesterase activity and are therefore able to detoxify organophosphate insecticides. A novel PLL representative, dubbed VmoLac, has been identified from the hyperthermophilic crenarchaeon Vulcanisaeta moutnovskia. Because of its intrinsic high thermal stability, VmoLac may constitute an appealing candidate for engineering studies with the aim of producing an efficient biodecontaminant for organophosphorus compounds and a bacterial antivirulence agent. In combination with biochemical studies, structural information will allow the identification of the residues involved in substrate specificity and an understanding of the enzymatic catalytic mechanisms. Here, the expression, purification, crystallization and X-ray data collection at 2.4 Å resolution of VmoLac are reported.

KEYWORDS:

Vulcanisaeta moutnovskia; extremophiles; lactonases; molecular promiscuity; organophosphorus; phosphotriesterases; quorum sensing

PMID:
24192357
PMCID:
PMC3818041
DOI:
10.1107/S1744309113024846
[Indexed for MEDLINE]
Free PMC Article

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