8hkg

Crystal structure of glycosidic hydrolase family 10 (GH10) xylanase XynA contains an additional proline-rich sequence in the C-terminus

spinqualitylabelsall models 8hkg, resolution 2.56Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8hkg is a 2 chain structure with sequence from Uncultured organism. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.56Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function L7UY53_9ZZZZ Publication Abstract from PubMed 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. Effectiveness of ruminal xylanase with an extra proline-rich C-terminus on lignocellulosic biomass degradation.,Dong R, Liao M, Liu X, Penttinen L, Hakulinen N, Qin X, Wang X, Huang H, Luo H, Yao B, Bai Y, Tu T Bioresour Technol. 2023 Mar;372:128695. doi: 10.1016/j.biortech.2023.128695. Epub , 2023 Jan 30. PMID:36731612 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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