5Z6P

The crystal structure of an agarase, AgWH50C

5Z6P の概要

• エントリーDOI: 10.2210/pdb5z6p/pdb
• 分子名称: B-agarase (2 entities in total)
• 機能のキーワード: glucoside hydrolase 50 family, agarase activity, hydrolase
• 由来する生物種: Agarivorans gilvus (Agarivorans sp. WH0801)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 173648.02

構造登録者

Mao, X.,Zhou, J.,Zhang, P.,Zhang, L.,Zhang, J.,Li, Y. (登録日: 2018-01-24, 公開日: 2019-01-02, 最終更新日: 2024-11-13)

主引用文献

Zhang, P.,Zhang, J.,Zhang, L.,Sun, J.,Li, Y.,Wu, L.,Zhou, J.,Xue, C.,Mao, X.
Structure-based design of agarase AgWH50C from Agarivorans gilvus WH0801 to enhance thermostability.
Appl. Microbiol. Biotechnol., 103:1289-1298, 2019

PubMed Abstract: AgWH50C, an exo-β-agarase of GH50 isolated from Agarivorans gilvus WH0801, plays a key role in the enzymatic production of neoagarobiose, which has great application prospect in the cosmetics and pharmaceutical industry. In contrast, the poor thermostability becomes the main obstructive factor of glycoside hydrolase (GH) family 50 agarases, including AgWH50C. Herein, based on the AgWH50C crystal structure, we designed several mutants by a multiple cross-linked rational design protocol used thermostability predicting softwares ETSS, PoPMuSiC, and HotMuSiC. To our surprise, the mutant K621F increased its relative activity by as much as 45% and the optimal temperature increased to 38 °C compared to that of wild-type, AgWH50C (30 °C). The thermostability of K621F also exhibited a substantial improvement. Considering that the gelling temperature of the agarose is higher than 35 °C, K621F can be used to hydrolyze agarose for neoagarobiose production.

PubMed: 30523371
DOI: 10.1007/s00253-018-9540-1

実験手法

X-RAY DIFFRACTION (2.061 Å)