3S2Z

Crystal structure of the Lactobacillus johnsonii cinnamoyl esterase LJ0536 S106A mutant in complex with caffeic acid

3S2Z の概要

• エントリーDOI: 10.2210/pdb3s2z/pdb
• 関連するPDBエントリー: 3PF8 3PF9 3PFB 3PFC
• 分子名称: Cinnamoyl esterase, CHLORIDE ION, CAFFEIC ACID, ... (4 entities in total)
• 機能のキーワード: alpha/beta hydrolase fold, esterase, hydrolase, cinnamoyl/feruloyl esterase, hydroxycinammates
• 由来する生物種: Lactobacillus johnsonii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60948.57

構造登録者

Stogios, P.J.,Lai, K.K.,Vu, C.,Xu, X.,Cui, H.,Molloy, S.,Gonzalez, C.F.,Yakunin, A.,Savchenko, A. (登録日: 2011-05-17, 公開日: 2011-08-31, 最終更新日: 2023-09-13)

主引用文献

Lai, K.K.,Stogios, P.J.,Vu, C.,Xu, X.,Cui, H.,Molloy, S.,Savchenko, A.,Yakunin, A.,Gonzalez, C.F.
An inserted alpha/beta subdomain shapes the catalytic pocket of Lactobacillus johnsonii cinnamoyl esterase.
Plos One, 6:e23269-e23269, 2011

PubMed Abstract: Microbial enzymes produced in the gastrointestinal tract are primarily responsible for the release and biochemical transformation of absorbable bioactive monophenols. In the present work we described the crystal structure of LJ0536, a serine cinnamoyl esterase produced by the probiotic bacterium Lactobacillus johnsonii N6.2.

PubMed: 21876742
DOI: 10.1371/journal.pone.0023269

実験手法

X-RAY DIFFRACTION (1.76 Å)