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嗜热真细菌非蛋白酶解栖热菌HG102来源的β-糖苷酶热稳定性的结构基础

Structural basis for thermostability of beta-glycosidase from the thermophilic eubacterium Thermus nonproteolyticus HG102.

作者信息

Wang Xinquan, He Xiangyuan, Yang Shoujun, An Xiaomin, Chang Wenrui, Liang Dongcai

机构信息

National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.

出版信息

J Bacteriol. 2003 Jul;185(14):4248-55. doi: 10.1128/JB.185.14.4248-4255.2003.

DOI:10.1128/JB.185.14.4248-4255.2003
PMID:12837801
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC164863/
Abstract

The three-dimensional structure of a thermostable beta-glycosidase (Gly(Tn)) from the thermophilic eubacterium Thermus nonproteolyticus HG102 was determined at a resolution of 2.4 A. The core of the structure adopts the (betaalpha)(8) barrel fold. The sequence alignments and the positions of the two Glu residues in the active center indicate that Gly(Tn) belongs to the glycosyl hydrolases of retaining family 1. We have analyzed the structural features of Gly(Tn) related to the thermostability and compared its structure with those of other mesophilic glycosidases from plants, eubacteria, and hyperthermophilic enzymes from archaea. Several possible features contributing to the thermostability of Gly(Tn) were elucidated.

摘要

嗜热真细菌嗜热栖热放线菌HG102的一种热稳定β-糖苷酶（Gly(Tn)）的三维结构在2.4埃的分辨率下得以确定。该结构的核心采用（βα）8桶状折叠。活性中心两个Glu残基的序列比对和位置表明，Gly(Tn)属于保留型家族1的糖基水解酶。我们分析了与热稳定性相关的Gly(Tn)的结构特征，并将其结构与来自植物、真细菌的其他嗜温糖苷酶以及古细菌的嗜热酶的结构进行了比较。阐明了几种可能有助于Gly(Tn)热稳定性的特征。