8HKG

Crystal structure of glycosidic hydrolase family 10 (GH10) xylanase XynA contains an additional proline-rich sequence in the C-terminus

8HKG の概要

• エントリーDOI: 10.2210/pdb8hkg/pdb
• 分子名称: xylanase (2 entities in total)
• 機能のキーワード: glycosidic hydrolase family 10, xylanase, proline-rich region, hydrolase
• 由来する生物種: uncultured organism
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 88275.49

構造登録者

Dong, R.Y.,Tu, T. (登録日: 2022-11-26, 公開日: 2023-02-22, 最終更新日: 2024-10-30)

主引用文献

Dong, R.,Liao, M.,Liu, X.,Penttinen, L.,Hakulinen, N.,Qin, X.,Wang, X.,Huang, H.,Luo, H.,Yao, B.,Bai, Y.,Tu, T.
Effectiveness of ruminal xylanase with an extra proline-rich C-terminus on lignocellulosic biomass degradation.
Bioresour Technol, 372:128695-128695, 2023

PubMed Abstract: The efficient degradation of plant polysaccharides in agricultural waste requires xylanases with high catalytic activity. In this study, the C-terminal proline-rich GH10 xylanase XynA from sheep rumen was investigated using product analysis, structural characterization, truncated and site-directed mutagenesis, molecular dynamics simulation, and application evaluation, revealing that the proline-rich C-terminus contributes to the interaction at the substrate-binding pocket to reduce the binding free energy. Compared to the C-terminally truncated enzyme XynA-Tr, XynA has a more favorable conformation for proton transfer and affinity attack, facilitating the degradation of oligomeric and beechwood xylan without altering the hydrolysis pattern. Moreover, both the reduced sugar yield and weight loss of the pretreated wheat bran, corn cob, and corn stalk hydrolyzed by XynA for 12 h increased by more than 30 %. These findings are important to better understand the relationship between enzyme activities and their terminal regions and suggest candidate materials for lignocellulosic biomass utilization.

PubMed: 36731612
DOI: 10.1016/j.biortech.2023.128695

実験手法

X-RAY DIFFRACTION (2.56 Å)