5ZQJ
Crystal structure of beta-xylosidase from Bacillus pumilus
Summary for 5ZQJ
| Entry DOI | 10.2210/pdb5zqj/pdb |
| Descriptor | Beta-xylosidase, GLYCEROL (3 entities in total) |
| Functional Keywords | xylobiose hydrolysis, hydrolase |
| Biological source | Bacillus pumilus (Bacillus mesentericus) |
| Total number of polymer chains | 2 |
| Total formula weight | 124733.51 |
| Authors | |
| Primary citation | Hong, S.,Kyung, M.,Jo, I.,Kim, Y.R.,Ha, N.C. Structure-based protein engineering of bacterial beta-xylosidase to increase the production yield of xylobiose from xylose Biochem. Biophys. Res. Commun., 501:703-710, 2018 Cited by PubMed Abstract: Xylobiose consists of two molecules of xylose and has been highly recognized as a food supplement because it possesses high prebiotic functions. β-xylosidase exhibits enzymatic activity to hydrolyze xylobiose, and the enzyme can also catalyze the reverse reaction in the presence of high concentrations of xylose. Previously, β-xylosidase from Bacillus pumilus IPO (BpXynB), belonging to GH family 43, was employed to produce xylobiose from xylose. To improve the enzymatic efficiency, this study determined the high-resolution structure of BpXynB in a complex with xylobiose and engineered BpXynB based on the structures. The structure of BpXynB deciphered the residues involved in the recognition of the xylobiose. A site-directed mutation at the residue for xylobiose recognition increased the yield of xylobiose by 20% compared to a similar activity of the wild type enzyme. The complex structure of the mutant enzyme and xylobiose provided the structural basis for a higher yield of the engineered protein. This engineered enzyme would enable a higher economic production of xylobiose, and a similar engineering strategy could be applied within the same family of enzymes. PubMed: 29752942DOI: 10.1016/j.bbrc.2018.05.051 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.73 Å) |
Structure validation
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