5M60

Chaetomium thermophilum beta-1-3-glucanase

5M60 の概要

• エントリーDOI: 10.2210/pdb5m60/pdb
• 分子名称: Beta-1,3-glucanase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: cellulose, glucanase, fungus, thermostability, glucans, transferase
• 由来する生物種: Chaetomium thermophilum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 83204.73

構造登録者

Papageorgiou, A.C.,Chen, J.,Li, D. (登録日: 2016-10-23, 公開日: 2017-05-17, 最終更新日: 2024-10-09)

主引用文献

Papageorgiou, A.C.,Chen, J.,Li, D.
Crystal structure and biological implications of a glycoside hydrolase family 55 beta-1,3-glucanase from Chaetomium thermophilum.
Biochim. Biophys. Acta, 1865:1030-1038, 2017

PubMed Abstract: Crystal structures of a β-1,3-glucanase from the thermophilic fungus Chaetomium thermophilum were determined at 1.20 and 1.42Å resolution in the free and glucose-bound form, respectively. This is the third structure of a family 55 glycoside hydrolase (GH55) member and the second from a fungus. Based on comparative structural studies and site-directed mutagenesis, Glu654 is proposed as the catalytic acid residue. The substrate binding cleft exhibits restricted access on one side, rendering the enzyme as an exo-β-1,3-glucanase as confirmed also by thin layer chromatography experiments. A lack of stacking interactions was found at the substrate binding cleft, suggesting that interactions at positions -1, +1 and +2 are sufficient to orientate the substrate. A binding pocket was identified that could explain binding of branched laminarin and accumulation of laminaritriose.

PubMed: 28479293
DOI: 10.1016/j.bbapap.2017.05.002

実験手法

X-RAY DIFFRACTION (1.5 Å)