Structural perspectives of an engineered beta-1,4-xylanase with enhanced enhanced thermostability

文献类型： 外文期刊

第一作者： Chen, Chun-Chi

作者： Chen, Chun-Chi;Han, Xu;Lv, Pin;Peng, Wei;Huang, Chun-Hsiang;Gao, Jian;Zheng, Yingying;Yang, Yunyun;Guo, Rey-Ting;Luo, Huiying;Wang, Kun;Yao, Bin;Ko, Tzu-Ping;Peng, Wei;Yang, Yunyun;Zhang, Jianyu

作者机构：

关键词： beta-1;4-Xylanase;Crystal structure;Thermozyme;Protein engineering;Protein rigidity

期刊名称：JOURNAL OF BIOTECHNOLOGY （ 影响因子：3.307； 五年影响因子：3.778 ）

ISSN：

年卷期：

页码：

收录情况： SCI

摘要： The glycoside hydrolase 10 (GH10) xylanase from Streptomyces sp. 9 (XynAS9) can operate in a broad range of pH and temperature, and thus is a potential candidate for commercial applications. Recently, we engineered XynAS9 via mutating several residues in accordance with the consensus sequences of GH10 thermophilic xylanases in an attempt to improve the enzyme thermo stability and thermotolerance. The most promising effects were observed in the double mutant V81P/G82E. In order to investigate the molecular mechanism of the improved thermal profile of XynAS9, complex crystal structures of the wild type (WT) and mutant (MT) enzyme were solved at 1.88-2.05 A resolution. The structures reveal a classical GH10 (beta/alpha)(8) TIM-barrel fold. In MT XynAS9, E82 forms several interactions to its neighboring residues, which might aid in stabilizing the local structure. Furthermore, the MT structure showed lower B factors for individual residues compared to the WT structure, reflecting the increased MT protein rigidity. Analyses of the XynAS9 structures also delineate the detailed enzyme-substrate interaction network. More importantly, possible explanations for the enhanced thermal profiles of MT XynAS9 are proposed, which may be a useful strategy for enzyme engineering in the future. (C) 2014 Elsevier B.V. All rights reserved.

分类号： Q81

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