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

CORC > 天津工业生物技术研究所 > 结构生物学与蛋白酶学实验室郭瑞庭 > 期刊论文

	Structural perspectives of an engineered beta-1,4-xylanase with enhanced enhanced thermostability
	Chen, Chun-Chi 1; Luo, Huiying 2; Han, Xu 1; Lv, Pin 1; Ko, Tzu-Ping 3; Peng, Wei 1,4; Huang, Chun-Hsiang 1; Wang, Kun 2; Gao, Jian 1; Zheng, Yingying 1
刊名	JOURNAL OF BIOTECHNOLOGY
	2014-11-10
卷号	189 页码:175-182
关键词	beta-1,4-Xylanase Crystal structure Thermozyme Protein engineering Protein rigidity
英文摘要	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.
WOS标题词	Science & Technology ; Life Sciences & Biomedicine
类目[WOS]	Biotechnology & Applied Microbiology
研究领域[WOS]	Biotechnology & Applied Microbiology
关键词[WOS]	STREPTOMYCES SP S9 ; SUBSTRATE-BINDING ; CRYSTAL-STRUCTURE ; MICROBIAL XYLANASES ; CATALYTIC DOMAIN ; RATIONAL DESIGN ; SOFTWARE ; SUITE ; MODE
收录类别	SCI
语种	英语
WOS记录号	WOS:000344184900026
内容类型	期刊论文
源URL	[http://124.16.173.210/handle/834782/1402]
专题	天津工业生物技术研究所_结构生物学与蛋白酶学实验室郭瑞庭_期刊论文
作者单位	1.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Ind Enzymes Natl Engn Lab, Tianjin 300308, Peoples R China 2.Chinese Acad Agr Sci, Feed Res Inst, Minist Agr, Key Lab Feed Biotechnol, Beijing 100081, Peoples R China 3.Acad Sinica, Inst Biol Chem, Taipei 11529, Taiwan 4.Tianjin Univ Sci & Technol, Coll Biotechnol, Tianjin 300457, Peoples R China 5.Jilin Univ, Norman Bethune Med Sch, Dept Biochem, Changchun 130021, Peoples R China
推荐引用方式 GB/T 7714	Chen, Chun-Chi,Luo, Huiying,Han, Xu,et al. Structural perspectives of an engineered beta-1,4-xylanase with enhanced enhanced thermostability[J]. JOURNAL OF BIOTECHNOLOGY,2014,189:175-182.
APA	Chen, Chun-Chi.,Luo, Huiying.,Han, Xu.,Lv, Pin.,Ko, Tzu-Ping.,...&Guo, Rey-Ting.(2014).Structural perspectives of an engineered beta-1,4-xylanase with enhanced enhanced thermostability.JOURNAL OF BIOTECHNOLOGY,189,175-182.
MLA	Chen, Chun-Chi,et al."Structural perspectives of an engineered beta-1,4-xylanase with enhanced enhanced thermostability".JOURNAL OF BIOTECHNOLOGY 189(2014):175-182.