4RE0

Crystal structure of VmoLac in P622 space group

4RE0 の概要

• エントリーDOI: 10.2210/pdb4re0/pdb
• 関連するPDBエントリー: 4RDY 4RDZ
• 分子名称: Parathion hydrolase, COBALT (II) ION, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: lactonase, quorum sensing, parathion hydrolase, aryldialkylesterase, hydrolase
• 由来する生物種: Vulcanisaeta moutnovskia
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36510.65

構造登録者

Hiblot, J.,Bzdrenga, J.,Champion, C.,Gotthard, G.,Gonzalez, D.,Chabriere, E.,Elias, M. (登録日: 2014-09-20, 公開日: 2015-02-25, 最終更新日: 2025-03-26)

主引用文献

Hiblot, J.,Bzdrenga, J.,Champion, C.,Chabriere, E.,Elias, M.
Crystal structure of VmoLac, a tentative quorum quenching lactonase from the extremophilic crenarchaeon Vulcanisaeta moutnovskia.
Sci Rep, 5:8372-8372, 2015

PubMed Abstract: A new representative of the Phosphotriesterase-Like Lactonases (PLLs) family from the hyperthermophilic crenarchaeon Vulcanisaeta moutnovskia has been characterized and crystallized. VmoLac is a native, proficient lactonase with promiscuous, low phosphotriesterase activity. VmoLac therefore represents an interesting candidate for engineering studies, with the aim of developing an efficient bacterial quorum-quenching agent. Here, we provide an extensive biochemical and kinetic characterization of VmoLac and describe the X-ray structures of the enzyme bound to a fatty acid and to its cognate substrate 3-oxo-C10 AHL (Acyl-Homoserine Lactone). The structures highlight possible structural determinants that may be involved in its extreme thermal stability (Tm = 128 °C). Moreover, the structure reveals that the substrate binding mode of VmoLac significantly differs from those of its close homologues, possibly explaining the substrate specificity of the enzyme. Finally, we describe the specific interactions between the enzyme and its substrate, and discuss the possible lactone hydrolysis mechanism of VmoLac.

PubMed: 25670483
DOI: 10.1038/srep08372

実験手法

X-RAY DIFFRACTION (2.35 Å)