Structural and mutagenetic analyses of a 1,3-1,4-beta-glucanase from Paecilomyces thermophila
文献类型：期刊论文
| 作者 | Cheng, Ya-Shan1,2; Huang, Chun-Hsiang3; Chen, Chun-Chi3; Huang, Ting-Yung1,2; Ko, Tzu-Ping4; Huang, Jian-Wen6; Wu, Tzu-Hui6; Liu, Je-Ruei5,6,7; Guo, Rey-Ting2 |
| 刊名 | BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
 |
| 出版日期 | 2014-02-01 |
| 卷号 | 1844期号:2页码:366-373 |
| 关键词 | 1,3-1,4-beta-Glucanase 1,3(4)-beta-Glucanase PtLic16A Crystal structure |
| 英文摘要 | The thermostable 1,3-1,4-beta-glucanase PtLic16A from the fungus Paecilomyces thermophila catalyzes stringent hydrolysis of barley beta-glucan and lichenan with an outstanding efficiency and has great potential for broad industrial applications. Here, we report the crystal structures of PtLic16A and an inactive mutant E113A in ligand-free form and in complex with the ligands cellobiose, cellotetraose and glucotriose at 1.80 angstrom to 2.25 angstrom resolution. PtLic16A adopts a typical beta-jellyroll fold with a curved surface and the concave face forms an extended ligand binding cleft. These structures suggest that PtLic16A might carry out the hydrolysis via retaining mechanism with E113 and E118 serving as the nucleophile and general acid/base, respectively. Interestingly, in the structure of E113A/1,3-1,4-beta-glucotriose complex, the sugar bound to the - 1 subsite adopts an intermediate-like (alpha-anomeric) configuration. By combining all crystal structures solved here, a comprehensive binding mode for a substrate is proposed. These findings not only help understand the 1,3-1,4-beta-glucanase catalytic mechanism but also provide a basis for further enzymatic engineering. (C) 2013 Elsevier B.V. All rights reserved. |
| 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] | LICHENIFORMIS 1,3-1,4-BETA-D-GLUCAN 4-GLUCANOHYDROLASE ; SITE-DIRECTED MUTAGENESIS ; CRYSTAL-STRUCTURE ; THERMOSTABLE BETA-1,3-1,4-GLUCANASE ; PHANEROCHAETE-CHRYSOSPORIUM ; ESCHERICHIA-COLI ; LAMINARINASE 16A ; LICHENASE ; COMPLEX ; SUCCINOGENES |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000330489000009 |
| 源URL | [http://124.16.173.210/handle/834782/1331]  |
| 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.Genozyme Biotechnol Inc, Taipei 106, Taiwan 2.AsiaPac Biotechnol Co Ltd, Dongguan 523808, Peoples R China 3.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Ind Enzymes Natl Engn Lab, Tianjin 300308, Peoples R China 4.Acad Sinica, Inst Biol Chem, Taipei 115, Taiwan 5.Acad Sinica, Agr Biotechnol Res Ctr, Taipei 115, Taiwan 6.Natl Taiwan Univ, Inst Biotechnol, Taipei 106, Taiwan 7.Natl Taiwan Univ, Dept Anim Sci & Technol, Taipei 106, Taiwan |
| 推荐引用方式 GB/T 7714 | Cheng, Ya-Shan,Huang, Chun-Hsiang,Chen, Chun-Chi,et al. Structural and mutagenetic analyses of a 1,3-1,4-beta-glucanase from Paecilomyces thermophila[J]. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS,2014,1844(2):366-373. |
| APA | Cheng, Ya-Shan.,Huang, Chun-Hsiang.,Chen, Chun-Chi.,Huang, Ting-Yung.,Ko, Tzu-Ping.,...&Guo, Rey-Ting.(2014).Structural and mutagenetic analyses of a 1,3-1,4-beta-glucanase from Paecilomyces thermophila.BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS,1844(2),366-373. |
| MLA | Cheng, Ya-Shan,et al."Structural and mutagenetic analyses of a 1,3-1,4-beta-glucanase from Paecilomyces thermophila".BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS 1844.2(2014):366-373. |
入库方式： OAI收割
来源：天津工业生物技术研究所
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