Structural insight into potential cold adaptation mechanism through a psychrophilic glycoside hydrolase family 10 endo-β-1,4-xylanase

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• 作者：Yingying Zheng^a ; ¹ ; Yujie Li^a ; ¹ ; Weidong Liu^a ; ¹ ; Chun-Chi Chen^a ; Tzu-Ping Ko^b ; Miao He^a ; ^d ; Zhongxia Xu^a ; ^e ; Meixia Liu^a ; ^d ; Huiying Luo^c ; Rey-Ting Guo^a ; ^{guo_rt@tib.cas.cn" class="auth_mail" title="E-mail the corresponding author} ; Bin Yao^c ; ^{yaobin@caas-bio.net.cn" class="auth_mail" title="E-mail the corresponding author} ; Yanhe Ma^a ; ^{ma_yh@tib.cas.cn" class="auth_mail" title="E-mail the corresponding author}
• 关键词：Xylanase ; Xylobiose ; Psychrophilic ; Cold-adaptation
• 刊名：Journal of Structural Biology
• 出版年：2016
• 出版时间：March 2016
• 年：2016
• 卷：193
• 期：3
• 页码：206-211
• 全文大小：1350 K

文摘

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 Å resolution. The enzyme folds into a typical GH10 (β/α)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.