5XGZ
Metagenomic glucose-tolerant glycosidase
Summary for 5XGZ
| Entry DOI | 10.2210/pdb5xgz/pdb |
| Descriptor | Beta-glycosidase, GLYCEROL, NICKEL (II) ION, ... (5 entities in total) |
| Functional Keywords | beta-glycosidase, meta genome, thermostable enzyme, glucose-tolerant, hydrolase |
| Biological source | uncultured microorganism |
| Total number of polymer chains | 2 |
| Total formula weight | 105980.14 |
| Authors | Watanabe, M.,Matsuzawa, T.,Yaoi, K. (deposition date: 2017-04-19, release date: 2018-05-02, Last modification date: 2023-11-22) |
| Primary citation | Matsuzawa, T.,Watanabe, M.,Yaoi, K. Improved thermostability of a metagenomic glucose-tolerant beta-glycosidase based on its X-ray crystal structure. Appl.Microbiol.Biotechnol., 101:8353-8363, 2017 Cited by PubMed Abstract: MeBglD2, a metagenomic β-glycosidase, is stimulated by various saccharides, including D-glucose, D-xylose, and maltose, and it promotes the enzymatic saccharification of plant biomass. To improve the thermostability of MeBglD2, its X-ray crystal structure was analyzed, and the amino acid residues responsible for its thermostability were identified using the structural information. Mutations in His8, Asn59, and Gly295 improved the thermostability of MeBglD2, and the combination of these mutations resulted in the highest thermostability. Compared with wild-type MeBglD2, thermostable MeBglD2 mutants promoted plant biomass saccharification using Trichoderma reesei cellulase. In addition to thermostability, the thermostable mutants exhibited higher tolerance to ethanol, dimethyl sulfoxide, and copper ions, indicating that the MeBglD2 mutants generated in this study were improved in their tolerance to not only high temperature but also to organic solvents and metal ions. PubMed: 29063172DOI: 10.1007/s00253-017-8525-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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