Structural insight into potential cold adaptation mechanism through a psychrophilic glycoside hydrolase family 10 endo-beta-1,4-xylanase
文献类型: 外文期刊
第一作者: Zheng, Yingying
作者: Zheng, Yingying;Li, Yujie;Liu, Weidong;Chen, Chun-Chi;He, Miao;Xu, Zhongxia;Liu, Meixia;Guo, Rey-Ting;Ma, Yanhe;Ko, Tzu-Ping;Luo, Huiying;Yao, Bin;He, Miao;Liu, Meixia;Xu, Zhongxia
作者机构:
关键词: Xylanase;Xylobiose;Psychrophilic;Cold-adaptation
期刊名称:JOURNAL OF STRUCTURAL BIOLOGY ( 影响因子:2.867; 五年影响因子:4.474 )
ISSN:
年卷期:
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收录情况: SCI
摘要: The cold-adapted xylanases can catalyze at low temperature and hold great potential in food industry applications. Here we describe the first crystal structure of a cold-adapted glycoside hydrolase (GH) family 10 xylanase XynGR40 and its complex with xylobiose at 2.15 and 2.50 angstrom resolution. The enzyme folds into a typical GH10 (beta/alpha)(8) TIM-barrel, with E132 and E243 serving as the catalytic residues. The xylobiose was observed to occupy the -1 and -2 subsites. Structural comparison with a thermophilic GH10 xylanase highlighting various parameters that may explain the cold adaptation features were analyzed. Synergistic effects of the increased exposure of hydrophobic residues, the higher flexibility of substrate-binding residues, more flexible loops, and the ratios of special amino acid residues, may result in the cold adaptation of XynGR40. (C) 2015 Elsevier Inc. All rights reserved.
分类号: Q13
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