8HKG
Crystal structure of glycosidic hydrolase family 10 (GH10) xylanase XynA contains an additional proline-rich sequence in the C-terminus
Summary for 8HKG
| Entry DOI | 10.2210/pdb8hkg/pdb |
| Descriptor | xylanase (2 entities in total) |
| Functional Keywords | glycosidic hydrolase family 10, xylanase, proline-rich region, hydrolase |
| Biological source | uncultured organism |
| Total number of polymer chains | 2 |
| Total formula weight | 88275.49 |
| Authors | Dong, R.Y.,Tu, T. (deposition date: 2022-11-26, release date: 2023-02-22, Last modification date: 2024-10-30) |
| Primary citation | Dong, R.,Liao, M.,Liu, X.,Penttinen, L.,Hakulinen, N.,Qin, X.,Wang, X.,Huang, H.,Luo, H.,Yao, B.,Bai, Y.,Tu, T. Effectiveness of ruminal xylanase with an extra proline-rich C-terminus on lignocellulosic biomass degradation. Bioresour Technol, 372:128695-128695, 2023 Cited by PubMed Abstract: The efficient degradation of plant polysaccharides in agricultural waste requires xylanases with high catalytic activity. In this study, the C-terminal proline-rich GH10 xylanase XynA from sheep rumen was investigated using product analysis, structural characterization, truncated and site-directed mutagenesis, molecular dynamics simulation, and application evaluation, revealing that the proline-rich C-terminus contributes to the interaction at the substrate-binding pocket to reduce the binding free energy. Compared to the C-terminally truncated enzyme XynA-Tr, XynA has a more favorable conformation for proton transfer and affinity attack, facilitating the degradation of oligomeric and beechwood xylan without altering the hydrolysis pattern. Moreover, both the reduced sugar yield and weight loss of the pretreated wheat bran, corn cob, and corn stalk hydrolyzed by XynA for 12 h increased by more than 30 %. These findings are important to better understand the relationship between enzyme activities and their terminal regions and suggest candidate materials for lignocellulosic biomass utilization. PubMed: 36731612DOI: 10.1016/j.biortech.2023.128695 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.56 Å) |
Structure validation
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