5XZU

Crystal structure of GH10 xylanase from Bispora. sp MEY-1 with xylobiose

Summary for 5XZU

• Entry DOI: 10.2210/pdb5xzu/pdb
• Related PRD ID: PRD_900005
• Descriptor: Beta-xylanase, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: gh10 family, xylanase, hydrolase
• Biological source: Bispora sp. MEY-1
• Total number of polymer chains: 2
• Total formula weight: 76691.34

Authors

You, S.,Chen, C.C.,Tu, T.,Guo, R.T.,Luo, H.Y.,Yao, B. (deposition date: 2017-07-14, release date: 2018-05-02, Last modification date: 2024-11-06)

Primary citation

You, S.,Chen, C.C.,Tu, T.,Wang, X.,Ma, R.,Cai, H.Y.,Guo, R.T.,Luo, H.Y.,Yao, B.
Insight into the functional roles of Glu175 in the hyperthermostable xylanase XYL10C-Delta N through structural analysis and site-saturation mutagenesis.
Biotechnol Biofuels, 11:159-159, 2018

PubMed Abstract: Improving the hydrolytic performance of hemicellulases to degrade lignocellulosic biomass is of considerable importance for second-generation biorefinery. Xylanase, as the crucial hemicellulase, must be thermostable and have high activity for its potential use in the bioethanol industry. To obtain excellent xylanase candidates, it is necessary to understand the structure-function relationships to provide a meaningful reference to improve the enzyme properties. This study aimed to investigate the catalytic mechanism of a highly active hyperthermophilic xylanase variant, XYL10C-ΔN, for hemicellulose degradation.

PubMed: 29930705
DOI: 10.1186/s13068-018-1150-8

Experimental method

X-RAY DIFFRACTION (1.7 Å)