4C89

Crystal structure of carboxylesterase LpEst1 from Lactobacillus plantarum: high resolution model

4C89 の概要

• エントリーDOI: 10.2210/pdb4c89/pdb
• 関連するPDBエントリー: 4C87 4C88
• 分子名称: ESTERASE, GLYCEROL, MALONATE ION, ... (4 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: LACTOBACILLUS PLANTARUM
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 156606.84

構造登録者

Alvarez, Y.,Esteban-Torres, M.,Cortes-Cabrera, A.,Gago, F.,Acebron, I.,Benavente, R.,Mardo, K.,de-las-Rivas, B.,Munoz, R.,Mancheno, J.M. (登録日: 2013-09-30, 公開日: 2014-04-02, 最終更新日: 2024-11-06)

主引用文献

Alvarez, Y.,Esteban-Torres, M.,Cortes-Cabrera, A.,Gago, F.,Acebron, I.,Benavente, R.,Mardo, K.,De-Las-Rivas, B.,Munoz, R.,Mancheno, J.M.
Esterase Lpest1 from Lactobacillus Plantarum: A Novel and Atypical Member of the Alpha Beta Hydrolase Superfamily of Enzymes
Plos One, 9:92257-, 2014

PubMed Abstract: The genome of the lactic acid bacterium Lactobacillus plantarum WCFS1 reveals the presence of a rich repertoire of esterases and lipases highlighting their important role in cellular metabolism. Among them is the carboxylesterase LpEst1 a bacterial enzyme related to the mammalian hormone-sensitive lipase, which is known to play a central role in energy homeostasis. In this study, the crystal structure of LpEst1 has been determined at 2.05 Å resolution; it exhibits an αβ-hydrolase fold, consisting of a central β-sheet surrounded by α-helices, endowed with novel topological features. The structure reveals a dimeric assembly not comparable with any other enzyme from the bacterial hormone-sensitive lipase family, probably echoing the specific structural features of the participating subunits. Biophysical studies including analytical gel filtration and ultracentrifugation support the dimeric nature of LpEst1. Structural and mutational analyses of the substrate-binding pocket and active site together with biochemical studies provided insights for understanding the substrate profile of LpEst1 and suggested for the first time the conserved Asp173, which is adjacent to the nucleophile, as a key element in the stabilization of the loop where the oxyanion hole resides.

PubMed: 24663330
DOI: 10.1371/JOURNAL.PONE.0092257

実験手法

X-RAY DIFFRACTION (2.05 Å)