Structural and functional analyses of catalytic domain of GH10 xylanase from Thermoanaerobacterium saccharolyticum JW/SL-YS485
文献类型：期刊论文
| 作者 | Han, Xu1; Gao, Jian1; Shang, Na1; Huang, Chun-Hsiang1; Ko, Tzu-Ping2; Chen, Chun-Chi3; Chan, Hsiu-Chien1; Cheng, Ya-Shan4; Zhu, Zhen1; Wiegel, Juergen5 |
| 刊名 | PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
 |
| 出版日期 | 2013-07-01 |
| 卷号 | 81期号:7页码:1256-1265 |
| 关键词 | glycoside hydrolase xylanase crystal structure thermophilic |
| 英文摘要 | Xylanases are capable of decomposing xylans, the major components in plant cell wall, and releasing the constituent sugars for further applications. Because xylanase is widely used in various manufacturing processes, high specific activity, and thermostability are desirable. Here, the wild-type and mutant (E146A and E251A) catalytic domain of xylanase from Thermoanaerobacterium saccharolyticum JW/SL-YS485 (TsXylA) were expressed in Escherichia coli and purified subsequently. The recombinant protein showed optimal temperature and pH of 75 degrees C and 6.5, respectively, and it remained fully active even after heat treatment at 75 degrees C for 1 h. Furthermore, the crystal structures of apo-form wild-type TsXylA and the xylobiose-, xylotriose-, and xylotetraose-bound E146A and E251A mutants were solved by X-ray diffraction to high resolution (1.32-1.66 angstrom). The protein forms a classic (/)8 folding of typical GH10 xylanases. The ligands in substrate-binding groove as well as the interactions between sugars and active-site residues were clearly elucidated by analyzing the complex structures. According to the structural analyses, TsXylA utilizes a double displacement catalytic machinery to carry out the enzymatic reactions. In conclusion, TsXylA is effective under industrially favored conditions, and our findings provide fundamental knowledge which may contribute to further enhancement of the enzyme performance through molecular engineering. Proteins 2013; 81:1256-1265. (c) 2013 Wiley Periodicals, Inc. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 关键词[WOS] | BETA-XYLOSIDASE XYLC ; STRAIN JW/SL-YS485 ; PURIFICATION ; EXPRESSION ; SEQUENCE ; ENZYMES |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000320474100015 |
| 公开日期 | 2014-12-24 |
| 源URL | [http://124.16.173.210/handle/311007/553]  |
| 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.Acad Sinica, Inst Biol Chem, Taipei 11529, Taiwan 3.Chinese Acad Sci, CAS Key Lab Pathogen Microbiol & Immunol, Inst Microbiol, Beijing 100101, Peoples R China 4.AsiaPac Biotechnol Co Ltd, Dongguan 523808, Peoples R China 5.Univ Georgia, Dept Microbiol, Athens, GA 30602 USA 6.South China Agr Univ, Coll Food Sci, Guangzhou 510642, Guangdong, Peoples R China |
| 推荐引用方式 GB/T 7714 | Han, Xu,Gao, Jian,Shang, Na,et al. Structural and functional analyses of catalytic domain of GH10 xylanase from Thermoanaerobacterium saccharolyticum JW/SL-YS485[J]. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS,2013,81(7):1256-1265. |
| APA | Han, Xu.,Gao, Jian.,Shang, Na.,Huang, Chun-Hsiang.,Ko, Tzu-Ping.,...&Ma, Yanhe.(2013).Structural and functional analyses of catalytic domain of GH10 xylanase from Thermoanaerobacterium saccharolyticum JW/SL-YS485.PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS,81(7),1256-1265. |
| MLA | Han, Xu,et al."Structural and functional analyses of catalytic domain of GH10 xylanase from Thermoanaerobacterium saccharolyticum JW/SL-YS485".PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS 81.7(2013):1256-1265. |
入库方式： OAI收割
来源：天津工业生物技术研究所
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