5I77

Crystal structure of a beta-1,4-endoglucanase from Aspergillus niger

5I77 の概要

• エントリーDOI: 10.2210/pdb5i77/pdb
• 関連するPDBエントリー: 5I78 5I79
• 分子名称: Endo-beta-1, 4-glucanase, CALCIUM ION, TRIETHYLENE GLYCOL, ... (6 entities in total)
• 機能のキーワード: substrate binding, endoglucanase, hydrolase
• 由来する生物種: Aspergillus niger
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34793.09

構造登録者

Li, Y.J.,Liu, W.D.,Zheng, Y.Y.,Chen, C.C.,Guo, R.T. (登録日: 2016-02-17, 公開日: 2016-12-21, 最終更新日: 2024-11-13)

主引用文献

Yan, J.,Liu, W.,Li, Y.,Lai, H.L.,Zheng, Y.,Huang, J.W.,Chen, C.C.,Chen, Y.,Jin, J.,Li, H.,Guo, R.T.
Functional and structural analysis of Pichia pastoris-expressed Aspergillus niger 1,4-beta-endoglucanase
Biochem. Biophys. Res. Commun., 475:8-12, 2016

PubMed Abstract: Eukaryotic 1,4-β-endoglucanases (EC 3.2.1.4) have shown great potentials in many commercial applications because they effectively catalyze hydrolysis of cellulose, the main component of the plant cell wall. Here we expressed a glycoside hydrolase family (GH) 5 1,4-β-endoglucanase from Aspergillus niger (AnCel5A) in Pichia pastoris, which exhibits outstanding pH and heat stability. In order to further investigate the molecular mechanism of AnCel5A, apo-form and cellotetraose (CTT) complex enzyme crystal structures were solved to high resolution. AnCel5A folds into a typical (β/α)8-TIM barrel architecture, resembling other GH5 members. In the substrate binding cavity, CTT is found to bind to -4 - -1 subsites, and several polyethylene glycol molecules are found in positive subsites. In addition, several unique N-glycosylation motifs that may contribute to protein higher stability were observed from crystal structures. These results are of great importance for understanding the molecular mechanism of AnCel5A, and also provide guidance for further applications of the enzyme.

PubMed: 27154222
DOI: 10.1016/j.bbrc.2016.05.012

実験手法

X-RAY DIFFRACTION (1.8 Å)