6IFE

A Glycoside Hydrolase Family 43 beta-Xylosidase

Summary for 6IFE

• Entry DOI: 10.2210/pdb6ife/pdb
• Descriptor: Beta-xylosidase, GLYCEROL (3 entities in total)
• Functional Keywords: glycoside hydrolase family 43, beta-xylosidase, low-temperature activity, salt tolerance, hydrolase
• Biological source: Bacillus pumilus
• Total number of polymer chains: 2
• Total formula weight: 127668.86

Authors

Li, N.,Liu, Y.,Zhang, R.,Zhou, J.P.,Huang, Z.X. (deposition date: 2018-09-20, release date: 2019-03-13, Last modification date: 2023-11-22)

Primary citation

Zhang, R.,Li, N.,Liu, Y.,Han, X.,Tu, T.,Shen, J.,Xu, S.,Wu, Q.,Zhou, J.,Huang, Z.
Biochemical and structural properties of a low-temperature-active glycoside hydrolase family 43 beta-xylosidase: Activity and instability at high neutral salt concentrations.
Food Chem, 301:125266-125266, 2019

PubMed Abstract: β-Xylosidase, of the glycoside hydrolase family 43 from Bacillus sp. HJ14, was expressed in Escherichia coli. Recombinant β-xylosidase (rHJ14GH43) exhibited maximum activity at 25 °C, approximately 15, 45, and 88% of maximum activity at 0, 10, and 20 °C, respectively, and poor stability at temperatures over 20 °C. rHJ14GH43 showed moderate or high activity, but poor stability, in NaCl, KCl, NaNO, KNO, NaSO, and (NH)SO at concentrations from 3.0 to 30.0% (w/v). The crystal structure of rHJ14GH43 was resolved and showed higher structural flexibility due to fewer salt bridges and hydrogen bonds compared to mesophilic and thermophilic β-xylosidases. High structural flexibility is presumed to be a key factor for catalytic adaptations to low temperatures and high salt concentrations. Approximately one-third of the surface of rHJ14GH43 is positively charged, which may be the primary factor responsible for poor stability in high neutral salt environments.

PubMed: 31387037
DOI: 10.1016/j.foodchem.2019.125266

Experimental method

X-RAY DIFFRACTION (1.804 Å)