Structural Characterization of β-Xylosidase XynB2 from Geobacillus stearothermophilus CECT43: A Member of the Glycoside Hydrolase Family GH52
Ficheros
Identificadores
Compartir
Metadatos
Mostrar el registro completo del ítemAutor
Gavira, J.A.; Contreras Moyeja, Lellys Mariela; Alshamaa, Hassan Mohamad; Clemente Jiménez, Josefa María; Rodríguez Vico, Felipe; [et al.]Fecha
2024Resumen
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 al...
Palabra/s clave
crystallization of β-xylosidase
XynB2
Glycoside Hydrolase Family 52
Glycoside Hydrolase Family 116