5GM3

Crystal structure of FI-CMCase from Aspergillus aculeatus F-50

5GM3 の概要

• エントリーDOI: 10.2210/pdb5gm3/pdb
• 関連するPDBエントリー: 5GM4 5GM5
• 分子名称: Endoglucanase-1, ZINC ION, CACODYLATE ION, ... (4 entities in total)
• 機能のキーワード: substrate binding, hydrolase-inhibitor complex, hydrolase/inhibitor
• 由来する生物種: Aspergillus aculeatus
• 細胞内の位置: Secreted: P22669
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48628.98

構造登録者

Huang, J.W.,Liu, W.D.,Zheng, Y.Y.,Chen, C.C.,Guo, R.T. (登録日: 2016-07-12, 公開日: 2017-05-17, 最終更新日: 2024-11-13)

主引用文献

Huang, J.W.,Liu, W.,Lai, H.L.,Cheng, Y.S.,Zheng, Y.,Li, Q.,Sun, H.,Kuo, C.J.,Guo, R.T.,Chen, C.C.
Crystal structure and genetic modifications of FI-CMCase from Aspergillus aculeatus F-50
Biochem. Biophys. Res. Commun., 478:565-572, 2016

PubMed Abstract: Cellulose is the major component of the plant cell wall and the most abundant renewable biomass on earth, and its decomposition has proven to be very useful in many commercial applications. Endo-1,4-β-d-glucanase (EC 3.2.1.4; endoglucanase), which catalyzes the random hydrolysis of 1,4-β-glycosidic bonds of the cellulose main chain to cleave cellulose into smaller fragments, is the key cellulolytic enzyme. An endoglucanase isolated from Aspergillus aculeatus F-50 (FI-CMCase), which is classified into the glycoside hydrolase (GH) family 12, was demonstrated to be effectively expressed in the industrial strain Pichia pastoris. Here, the crystal structure and complex structures of P. pastoris-expressed FI-CMCase were solved to high resolution. The overall structure is analyzed and compared to other GH12 members. In addition, the substrate-surrounding residues were engineered to search for variants with improved enzymatic activity. Among 14 mutants constructed, one with two-fold increase in protein expression was identified, which possesses a potential to be further developed as a commercial enzyme product.

PubMed: 27470581
DOI: 10.1016/j.bbrc.2016.07.101

実験手法

X-RAY DIFFRACTION (1.59 Å)