首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Crystallization and preliminary X-ray diffraction analysis of the lactonase VmoLac from Vulcanisaeta moutnovskia
【24h】

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

机译:Vulcanisaeta moutnovskia内酯酶VmoLac的结晶和初步X射线衍射分析

获取原文
获取原文并翻译 | 示例
获取外文期刊封面目录资料

摘要

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 hyperthermo-philic 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 angstrom resolution of VmoLac are reported.
机译:磷酸三酯酶样内酯酶(PLL)是天然的内酯酶,能够水解内酯,例如脂肪族内酯或酰基高丝氨酸内酯,它们参与细菌群体感应。此外,先前表征的PLL具有混杂的磷酸三酯酶活性,因此能够使有机磷酸酯杀虫剂解毒。已经从嗜热性crenarchaeon Vulcanisaeta moutnovskia中鉴定了一种名为VmoLac的新型PLL代表。由于其固有的高热稳定性,VmoLac可能成为工程研究的吸引人的候选物,目的是生产一种有效的有机磷化合物和细菌抗毒剂生物净化剂。与生化研究相结合,结构信息将允许鉴定底物特异性所涉及的残基并了解酶催化机理。在这里,报道了以2.4埃分辨率的VmoLac的表达,纯化,结晶和X射线数据收集。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号