@misc{10481/90920,
year = {2023},
month = {12},
url = {https://hdl.handle.net/10481/90920},
abstract = {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.},
organization = {Spanish Ministry of Science and Innovation/FEDER
funds Grant PID2020-116261GB-I00/AEI/10.13039/501100011033},
organization = {European Regional
Development Fund Andalucía 2014–2020 Grant UAL18-CTS-B032-A},
organization = {Own Research
and Transfer Plan 2020 of the University of Almeria Grant PPUENTE2020/006},
publisher = {MDPI},
keywords = {Crystallization of β-xylosidase},
keywords = {XynB2},
keywords = {Glycoside Hydrolase Family 52},
title = {Structural Characterization of β-Xylosidase XynB2 from Geobacillus stearothermophilus CECT43: A Member of the Glycoside Hydrolase Family GH52},
doi = {10.3390/cryst14010018},
author = {Gavira Gallardo, José Antonio and Contreras, Lellys M. and Alshamaa, Hassan Mohamad and Clemente Jiménez, Josefa María and Rodríguez Vico, Felipe and Las Heras Vázquez, Francisco Javier and Martínez Rodríguez, Sergio},
}