3CN7

Crystal Structure Analysis of the Carboxylesterase PA3859 from Pseudomonas aeruginosa PAO1- MONOCLINIC CRYSTAL FORM

3CN7 の概要

• エントリーDOI: 10.2210/pdb3cn7/pdb
• 関連するPDBエントリー: 1AUO 1AUR 1FJ2 3CN9
• 分子名称: Carboxylesterase, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID (3 entities in total)
• 機能のキーワード: alpha/beta hydrolase fold super-family, hydrolase
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 99270.14

構造登録者

Pesaresi, A.,Lamba, D. (登録日: 2008-03-25, 公開日: 2009-03-10, 最終更新日: 2024-11-13)

主引用文献

Pesaresi, A.,Lamba, D.
Insights into the fatty acid chain length specificity of the carboxylesterase PA3859 from Pseudomonas aeruginosa: A combined structural, biochemical and computational study.
Biochimie, 92:1787-1792, 2010

PubMed Abstract: The open reading frame PA3859 of Pseudomonas aeruginosa encodes an intracellular carboxylesterase belonging to a group of microbial enzymes (EC 3.1.1.1) that catalyze the hydrolysis of aliphatic and aromatic esters with a broad substrate specificity. With few exceptions, for this class of enzymes, belonging to the α/β-hydrolase fold superfamily, very little information is available regarding their biochemical activity and in vivo function. The X-ray crystal structure of recombinant PA3859 has been determined for two crystal forms (space groups P2(1) and P2(1)2(1)2). The kinetic properties of the enzyme were studied using p-nitrophenyl esters as substrates and data fitted to a surface dilution mixed micelle kinetic model. Enzymatic assays and computational docking simulations, pinpointed the enzyme's preference for esters of palmitic and/or stearic acids and provided insights into the enzyme-substrate favorable binding modes.

PubMed: 20850500
DOI: 10.1016/j.biochi.2010.09.001

実験手法

X-RAY DIFFRACTION (2.99 Å)