6M4E

Crystal structure of a GH1 beta-glucosidase from Hamamotoa singularis

6M4E の概要

• エントリーDOI: 10.2210/pdb6m4e/pdb
• 分子名称: Beta-galactosidase-like enzyme, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose, ... (6 entities in total)
• 機能のキーワード: galactooligosaccharide, transgalactosylation, beta-galactosidase, beta-glucosidase, hamamotoa singularis, structural protein, hydrolase
• 由来する生物種: Hamamotoa singularis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 69670.72

構造登録者

Uehara, R.,Iwamoto, R.,Aoki, S.,Yoshizawa, T.,Takano, K.,Matsumura, H.,Tanaka, S.-i. (登録日: 2020-03-06, 公開日: 2020-09-02, 最終更新日: 2024-10-30)

主引用文献

Uehara, R.,Iwamoto, R.,Aoki, S.,Yoshizawa, T.,Takano, K.,Matsumura, H.,Tanaka, S.I.
Crystal structure of a GH1 beta-glucosidase from Hamamotoa singularis.
Protein Sci., 29:2000-2008, 2020

PubMed Abstract: A GH1 β-glucosidase from the fungus Hamamotoa singularis (HsBglA) has high transgalactosylation activity and efficiently converts lactose to galactooligosaccharides. Consequently, HsBglA is among the most widely used enzymes for industrial galactooligosaccharide production. Here, we present the first crystal structures of HsBglA with and without 4'-galactosyllactose, a tri-galactooligosaccharide, at 3.0 and 2.1 Å resolutions, respectively. These structures reveal details of the structural elements that define the catalytic activity and substrate binding of HsBglA, and provide a possible interpretation for its high catalytic potency for transgalactosylation reaction.

PubMed: 32713015
DOI: 10.1002/pro.3916

実験手法

X-RAY DIFFRACTION (2.1 Å)