Structural Analysis of a Glycoside Hydrolase Family 11 Xylanase from Neocallimastix patriciarum

  • Cheng Y
  • Chen C
  • Huang C
  • et al.
N/ACitations
Citations of this article
9Readers
Mendeley users who have this article in their library.

This article is free to access.

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.

Cite

CITATION STYLE

APA

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

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free