3WDX

The complex structure of E113A with glucotriose

3WDX の概要

• エントリーDOI: 10.2210/pdb3wdx/pdb
• 関連するPDBエントリー: 3WDT 3WDU 3WDV 3WDW 3WDY
• 分子名称: Beta-1,3-1,4-glucanase, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-3)-alpha-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: 1, 3-1, 4-beta-glucanase, 3(4)-beta-glucanase, ptlic16a, beta-jellyroll fold, hydrolase
• 由来する生物種: Paecilomyces (Paecilomyces thermophila)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 66350.04

構造登録者

Cheng, Y.S.,Huang, C.H.,Chen, C.C.,Huang, T.Y.,Ko, T.P.,Huang, J.W.,Wu, T.H.,Liu, J.R.,Guo, R.T. (登録日: 2013-06-25, 公開日: 2014-07-09, 最終更新日: 2024-10-30)

主引用文献

Cheng, Y.S.,Huang, C.H.,Chen, C.C.,Huang, T.Y.,Ko, T.P.,Huang, J.W.,Wu, T.H.,Liu, J.R.,Guo, R.T.
Structural and mutagenetic analyses of a 1,3-1,4-beta-glucanase from Paecilomyces thermophila
Biochim.Biophys.Acta, 1844:366-373, 2014

PubMed Abstract: The thermostable 1,3-1,4-β-glucanase PtLic16A from the fungus Paecilomyces thermophila catalyzes stringent hydrolysis of barley β-glucan and lichenan with an outstanding efficiency and has great potential for broad industrial applications. Here, we report the crystal structures of PtLic16A and an inactive mutant E113A in ligand-free form and in complex with the ligands cellobiose, cellotetraose and glucotriose at 1.80Å to 2.25Å resolution. PtLic16A adopts a typical β-jellyroll fold with a curved surface and the concave face forms an extended ligand binding cleft. These structures suggest that PtLic16A might carry out the hydrolysis via retaining mechanism with E113 and E118 serving as the nucleophile and general acid/base, respectively. Interestingly, in the structure of E113A/1,3-1,4-β-glucotriose complex, the sugar bound to the -1 subsite adopts an intermediate-like (α-anomeric) configuration. By combining all crystal structures solved here, a comprehensive binding mode for a substrate is proposed. These findings not only help understand the 1,3-1,4-β-glucanase catalytic mechanism but also provide a basis for further enzymatic engineering.

PubMed: 24262091
DOI: 10.1016/j.bbapap.2013.11.005

実験手法

X-RAY DIFFRACTION (1.9 Å)