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

Julien Hiblot, Guillaume Gotthard, Charlotte Champion, Eric Chabriere, Mikael Elias

Research output: Contribution to journalArticlepeer-review

17 Scopus citations


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 2.4Å resolution of VmoLac are reported.

Original languageEnglish (US)
Pages (from-to)1235-1238
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number11
StatePublished - Nov 2013
Externally publishedYes


  • Extremophiles
  • Lactonases
  • Molecular promiscuity
  • Organophosphorus
  • Phosphotriesterases
  • Quorum sensing
  • Vulcanisaeta moutnovskia


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