| Autor: |
Jose Antonio Gavira, Lellys M. Contreras, Hassan Mohamad Alshamaa, Josefa María Clemente-Jiménez, Felipe Rodríguez-Vico, Francisco Javier Las Heras-Vázquez, Sergio Martínez-Rodríguez |
| Jazyk: |
angličtina |
| Rok vydání: |
2023 |
| Předmět: |
|
| Zdroj: |
Crystals, Vol 14, Iss 1, p 18 (2023) |
| Druh dokumentu: |
article |
| ISSN: |
2073-4352 |
| DOI: |
10.3390/cryst14010018 |
| Popis: |
β-xylosidases (4-β-d-xylan xylohydrolase, E.C. 3.2.1.37) are glycoside hydrolases (GH) catalyzing the hydrolysis of (1→4)-β-d-xylans, allowing for the removal of β-d-xylose residues from its non-reducing termini. Together with other xylan-degrading enzymes, β-xylosidases are involved in the enzymatic hydrolysis of lignocellulosic biomass, making them highly valuable in the biotechnological field. Whereas different GH families are deeply characterized from a structural point of view, the GH52 family has been barely described. In this work, we report the 2.25 Å resolution structure of Geobacillus stearothermophilus CECT43 XynB2, providing the second structural characterization for this GH family. A plausible dynamic loop closing the entrance of the catalytic cleft is proposed based on the comparison of the available GH52 structures, suggesting the relevance of a dimeric structure for members of this family. The glycone specificity at the −1 site for GH52 and GH116 members is also explained by our structural studies. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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