6M4E
Crystal structure of a GH1 beta-glucosidase from Hamamotoa singularis
Summary for 6M4E
| Entry DOI | 10.2210/pdb6m4e/pdb |
| Descriptor | 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) |
| Functional Keywords | galactooligosaccharide, transgalactosylation, beta-galactosidase, beta-glucosidase, hamamotoa singularis, structural protein, hydrolase |
| Biological source | Hamamotoa singularis |
| Total number of polymer chains | 1 |
| Total formula weight | 69670.72 |
| Authors | Uehara, R.,Iwamoto, R.,Aoki, S.,Yoshizawa, T.,Takano, K.,Matsumura, H.,Tanaka, S.-i. (deposition date: 2020-03-06, release date: 2020-09-02, Last modification date: 2024-10-30) |
| Primary citation | 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 Cited by 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: 32713015DOI: 10.1002/pro.3916 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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