7XRT

Bacteroides thetaiotaomicron ferulic acid esterase (BT_4077)

7XRT の概要

• エントリーDOI: 10.2210/pdb7xrt/pdb
• 関連するPDBエントリー: 7XRV
• 分子名称: Ferulic acid esterase, CALCIUM ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
• 機能のキーワード: esterase, hydrolase
• 由来する生物種: Bacteroides thetaiotaomicron VPI-5482
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 334862.63

構造登録者

Du, G.M.,Wang, Y.L.,Xin, F.J. (登録日: 2022-05-11, 公開日: 2023-11-22, 最終更新日: 2024-11-06)

主引用文献

Du, G.,Wang, Y.,Zhang, Y.,Yu, H.,Liu, S.,Ma, X.,Cao, H.,Wei, X.,Wen, B.,Li, Z.,Fan, S.,Zhou, H.,Xin, F.
Structural insights into the oligomeric effects on catalytic activity of a decameric feruloyl esterase and its application in ferulic acid production.
Int.J.Biol.Macromol., 253:126540-126540, 2023

PubMed Abstract: Oligomeric feruloyl esterase (FAE) has great application prospect in industry due to its potentially high stability and fine-tuned activity. However, the relationship between catalytic capability and oligomeric structure remains undetermined. Here we identified and characterized a novel, cold-adapted FAE (BtFae) derived from Bacteroides thetaiotaomicron. Structural studies unraveled that BtFae adopts a barrel-like decameric architecture unique in esterase families. By disrupting the interface, the monomeric variant exhibited significantly reduced catalytic activity and stability toward methyl ferulate, potentially due to its impact on the flexibility of the catalytic triad. Additionally, our results also showed that the monomerization of BtFae severely decreased the ferulic acid release from de-starched wheat bran and insoluble wheat arabinoxylan by 75 % and 80 %, respectively. Collectively, this study revealed novel connections between oligomerization and FAE catalytic function, which will benefit for further protein engineering of FAEs at the quaternary structure level for improved industrial applications.

PubMed: 37634773
DOI: 10.1016/j.ijbiomac.2023.126540

実験手法

X-RAY DIFFRACTION (2.007 Å)