2VC5

Structural basis for natural lactonase and promiscuous phosphotriesterase activities

2VC5 の概要

• エントリーDOI: 10.2210/pdb2vc5/pdb
• 関連するPDBエントリー: 2VC7
• 分子名称: ARYLDIALKYLPHOSPHATASE, FE (II) ION, COBALT (II) ION, ... (6 entities in total)
• 機能のキーワード: phosphotriesterase, promiscuous activities, enzyme evolution, hyperthermophilic, lactonase, hydrolase, biotechnology, quorum sensing
• 由来する生物種: SULFOLOBUS SOLFATARICUS
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 144574.32

構造登録者

Elias, M.,Dupuy, J.,Merone, L.,Mandrich, L.,Moniot, S.,Lecomte, C.,Rossi, M.,Masson, P.,Manco, G.,Chabriere, E. (登録日: 2007-09-18, 公開日: 2008-04-15, 最終更新日: 2023-12-13)

主引用文献

Elias, M.,Dupuy, J.,Merone, L.,Mandrich, L.,Porzio, E.,Moniot, S.,Rochu, D.,Lecomte, C.,Rossi, M.,Masson, P.,Manco, G.,Chabriere, E.
Structural Basis for Natural Lactonase and Promiscuous Phosphotriesterase Activities.
J.Mol.Biol., 379:1017-, 2008

PubMed Abstract: Organophosphates are the largest class of known insecticides, several of which are potent nerve agents. Consequently, organophosphate-degrading enzymes are of great scientific interest as bioscavengers and biodecontaminants. Recently, a hyperthermophilic phosphotriesterase (known as SsoPox), from the Archaeon Sulfolobus solfataricus, has been isolated and found to possess a very high lactonase activity. Here, we report the three-dimensional structures of SsoPox in the apo form (2.6 A resolution) and in complex with a quorum-sensing lactone mimic at 2.0 A resolution. The structure also reveals an unexpected active site topology, and a unique hydrophobic channel that perfectly accommodates the lactone substrate. Structural and mutagenesis evidence allows us to propose a mechanism for lactone hydrolysis and to refine the catalytic mechanism established for phosphotriesterases. In addition, SsoPox structures permit the correlation of experimental lactonase and phosphotriesterase activities and this strongly suggests lactonase activity as the cognate function of SsoPox. This example demonstrates that promiscuous activities probably constitute a large and efficient reservoir for the creation of novel catalytic activities.

PubMed: 18486146
DOI: 10.1016/J.JMB.2008.04.022

実験手法

X-RAY DIFFRACTION (2.6 Å)