5X39

Solution structure of the Family 1 carbohydrate-binding module Q2A mutant with mannosylated Ser3

5X39 の概要

• エントリーDOI: 10.2210/pdb5x39/pdb
• 関連するPDBエントリー: 5X34 5X35 5X36 5X37 5X38 5X3c
• NMR情報: BMRB: 36055
• 分子名称: Exoglucanase 1, alpha-D-mannopyranose (2 entities in total)
• 機能のキーワード: carbohydrate binding, hydrolase
• 由来する生物種: Hypocrea jecorina
• 細胞内の位置: Secreted: P62694
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3869.23

構造登録者

Feng, Y.,Tan, Z. (登録日: 2017-02-04, 公開日: 2017-05-31, 最終更新日: 2024-10-16)

主引用文献

Chaffey, P.K.,Guan, X.,Chen, C.,Ruan, Y.,Wang, X.,Tran, A.H.,Koelsch, T.N.,Cui, Q.,Feng, Y.,Tan, Z.
Structural Insight into the Stabilizing Effect of O-Glycosylation
Biochemistry, 56:2897-2906, 2017

PubMed Abstract: Protein glycosylation has been shown to have a variety of site-specific and glycan-specific effects, but so far, the molecular logic that leads to such observations has been elusive. Understanding the structural changes that occur and being able to correlate those with the physical properties of the glycopeptide are valuable steps toward being able to predict how specific glycosylation patterns will affect the stability of glycoproteins. By systematically comparing the structural features of the O-glycosylated carbohydrate-binding module of a Trichoderma reesei-derived Family 7 cellobiohydrolase, we were able to develop a better understanding of the influence of O-glycan structure on the molecule's physical stability. Our results indicate that the previously observed stabilizing effects of O-glycans come from the introduction of new bonding interactions to the structure and increased rigidity, while the decreased stability seemed to result from the impaired interactions and increased conformational flexibility. This type of knowledge provides a powerful and potentially general mechanism for improving the stability of proteins through glycoengineering.

PubMed: 28494147
DOI: 10.1021/acs.biochem.7b00195

実験手法

SOLUTION NMR