4G2D

Crystal structure of the hyperthermophilic Sulfolobus islandicus PLL SisLac

4G2D の概要

• エントリーDOI: 10.2210/pdb4g2d/pdb
• 関連するPDBエントリー: 2vc5 2vc7 3uf9
• 分子名称: Aryldialkylphosphatase, COBALT (II) ION, FE (II) ION, ... (4 entities in total)
• 機能のキーワード: promiscuous activities, hyperthermophilic, hydrolase, phosphotriesterase-like lactonases, quorum sensing, quorum-quenching, bioscavengers, (alpha/beta )8-barrel fold, lactonase, phosphotriesterase, lysine nz-carboxylic acid
• 由来する生物種: Sulfolobus islandicus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35870.86

構造登録者

Gotthard, G.,Hiblot, J.,Elias, M.,Chabriere, E. (登録日: 2012-07-11, 公開日: 2012-10-24, 最終更新日: 2023-12-06)

主引用文献

Hiblot, J.,Gotthard, G.,Chabriere, E.,Elias, M.
Structural and enzymatic characterization of the lactonase SisLac from Sulfolobus islandicus
Plos One, 7:e47028-e47028, 2012

PubMed Abstract: A new member of the Phosphotriesterase-Like Lactonases (PLL) family from the hyperthermophilic archeon Sulfolobus islandicus (SisLac) has been characterized. SisLac is a native lactonase that exhibits a high promiscuous phosphotriesterase activity. SisLac thus represents a promising target for engineering studies, exhibiting both detoxification and bacterial quorum quenching abilities, including human pathogens such as Pseudomonas aeruginosa.

PubMed: 23071703
DOI: 10.1371/journal.pone.0047028

実験手法

X-RAY DIFFRACTION (2.7 Å)