7YHF

Solution structure of S3C mutant of carbohydrate binding module (CBM) of the glycoside hydrolase Family 7 cellobiohydrolase from Trichoderma reesei

7YHF の概要

• エントリーDOI: 10.2210/pdb7yhf/pdb
• 関連するPDBエントリー: 5X34 5X36 7YHG 7YHH 7YHI
• 分子名称: Exoglucanase 1 (1 entity in total)
• 機能のキーワード: carbohydrate binding, hydrolase
• 由来する生物種: Trichoderma reesei
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3762.19

構造登録者

Chen, C.,Feng, Y.,Tan, Z. (登録日: 2022-07-13, 公開日: 2023-07-19, 最終更新日: 2024-10-30)

主引用文献

Chen, C.,Ma, B.,Wang, Y.,Cui, Q.,Yao, L.,Li, Y.,Chen, B.,Feng, Y.,Tan, Z.
Structural insight into why S-linked glycosylation cannot adequately mimic the role of natural O-glycosylation.
Int.J.Biol.Macromol., 253:126649-126649, 2023

PubMed Abstract: There is an increasing interest in using S-glycosylation as a replacement for the more commonly occurring O-glycosylation, aiming to enhance the resistance of glycans against chemical hydrolysis and enzymatic degradation. However, previous studies have demonstrated that these two types of glycosylation exert distinct effects on protein properties and functions. In order to elucidate the structural basis behind the observed differences, we conducted a systematic and comparative analysis of 6 differently glycosylated forms of a model glycoprotein, CBM, using NMR spectroscopy and molecular dynamic simulations. Our findings revealed that the different stabilizing effects of S- and O-glycosylation could be attributed to altered hydrogen-bonding capability between the glycan and the polypeptide chain, and their diverse impacts on binding affinity could be elucidated by examining the interactions and motion dynamics of glycans in substrate-bound states. Overall, this study underscores the pivotal role of the glycosidic linkage in shaping the function of glycosylation and advises caution when switching glycosylation types in protein glycoengineering.

PubMed: 37666405
DOI: 10.1016/j.ijbiomac.2023.126649

実験手法

SOLUTION NMR