Structural Characterization of β-Xylosidase XynB2 from Geobacillus stearothermophilus CECT43: A Member of the Glycoside Hydrolase Family GH52

• Published in: Crystals (Basel) Vol. 14; no. 1; p. 18
• Main Authors: Gavira, Jose Antonio, Contreras, Lellys M., Alshamaa, Hassan Mohamad, Clemente-Jiménez, Josefa María, Rodríguez-Vico, Felipe, Las Heras-Vázquez, Francisco Javier, Martínez-Rodríguez, Sergio
• Format: Journal Article
• Language: English
• Published: Basel MDPI AG 01.01.2024
• Subjects: Biocatalysts; Blood vessels; Cloning; Crystallization; crystallization of β-xylosidase; Crystals; Data collection; Enzymes; Glycerol; Glycosidases; Glycoside Hydrolase Family 116; Glycoside Hydrolase Family 52; Glycosides; Hydrolysis; Lignocellulose; Proteins; Structural analysis; XynB2
• ISSN: 2073-4352; 2073-4352
• DOI: 10.3390/cryst14010018

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.