Abstract
Background: Thermophilic xylanases are valuable in many industrial applications. Results: The structures of a xylanase XynCDBFV and its complex with xylooligosaccharides were determined, and its N-terminal region (NTR) contributes to thermostability. Conclusion: NTR may stabilize the overall protein folding of XynCDBFV. Significance: The structural and functional investigation of unprecedented NTR of XynCDBFV provides a new insight into the molecular basis of thermophilic xylanases. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
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CITATION STYLE
Cheng, Y.-S., Chen, C.-C., Huang, C.-H., Ko, T.-P., Luo, W., Huang, J.-W., … Guo, R.-T. (2014). Structural Analysis of a Glycoside Hydrolase Family 11 Xylanase from Neocallimastix patriciarum. Journal of Biological Chemistry, 289(16), 11020–11028. https://doi.org/10.1074/jbc.m114.550905
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