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 2.4Å resolution of VmoLac are reported.
Original language | English (US) |
---|---|
Pages (from-to) | 1235-1238 |
Number of pages | 4 |
Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Volume | 69 |
Issue number | 11 |
DOIs | |
State | Published - Nov 2013 |
Externally published | Yes |
Keywords
- Extremophiles
- Lactonases
- Molecular promiscuity
- Organophosphorus
- Phosphotriesterases
- Quorum sensing
- Vulcanisaeta moutnovskia