Diverse substrate recognition mechanism revealed by Thermotoga maritima Cel5A structures in complex with cellotetraose, cellobiose and mannotriose
文献类型：期刊论文
| 作者 | Wu, Tzu-Hui1; Huang, Chun-Hsiang3; Ko, Tzu-Ping4; Lai, Hui-Lin7; Ma, Yanhe3; Chen, Chun-Chi5; Cheng, Ya-Shan1,7; Liu, Je-Ruei1,2,6; Guo, Rey-Ting3 |
| 刊名 | BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
 |
| 出版日期 | 2011-12-01 |
| 卷号 | 1814期号:12页码:1832-1840 |
| 关键词 | Cellulose Cellulase Biofuel Crystal structure Synchrotron radiation |
| 英文摘要 | The hyperthermophilic endoglucanase Cel5A from Thermotoga maritime can find applications in lignocellulosic biofuel production, because it catalyzes the hydrolysis of glucan- and mannan-based polysaccharides. Here, we report the crystal structures in apo-form and in complex with three ligands, cellotetraose, cellobiose and mannotriose, at 1,29 angstrom to 2.40 angstrom resolution. The open carbohydrate-binding cavity which can accommodate oligosaccharide substrates with extensively branched chains explained the dual specificity of the enzyme. Combining our structural information and the previous kinetic data, it is suggested that this enzyme prefers beta-glucosyl and beta-mannosyl moieties at the reducing end and uses two conserved catalytic residues, E253 (nucleophile) and E136 (general acid/base), to hydrolyze the glycosidic bonds. Moreover, our results also suggest that the wide spectrum of Tm_Cel5A substrates might be due to the lack of steric hindrance around the C2-hydroxyl group of the glucose or mannose unit from active-site residues. (C) 2011 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] | GLYCOSYL HYDROLASES ; CRYSTAL-STRUCTURE ; FAMILY 5 ; ENDOGLUCANASE ; SOFTWARE ; HYDROLYSIS ; REFINEMENT ; PROTEINS ; DENSITY ; ETHANOL |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000298363200027 |
| 公开日期 | 2011-08-31 |
| 源URL | [http://localhost/handle/0/165]  |
| 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.Natl Taiwan Univ, Inst Biotechnol, Taipei 106, Taiwan 2.Natl Taiwan Univ, Dept Anim Sci & Technol, Taipei 106, Taiwan 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, Inst Biomed Sci, Taipei 115, Taiwan 6.Acad Sinica, Agr Biotechnol Res Ctr, Taipei 115, Taiwan 7.Genozyme Biotechnol Inc, Taipei 106, Taiwan |
| 推荐引用方式 GB/T 7714 | Wu, Tzu-Hui,Huang, Chun-Hsiang,Ko, Tzu-Ping,et al. Diverse substrate recognition mechanism revealed by Thermotoga maritima Cel5A structures in complex with cellotetraose, cellobiose and mannotriose[J]. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS,2011,1814(12):1832-1840. |
| APA | Wu, Tzu-Hui.,Huang, Chun-Hsiang.,Ko, Tzu-Ping.,Lai, Hui-Lin.,Ma, Yanhe.,...&Guo, Rey-Ting.(2011).Diverse substrate recognition mechanism revealed by Thermotoga maritima Cel5A structures in complex with cellotetraose, cellobiose and mannotriose.BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS,1814(12),1832-1840. |
| MLA | Wu, Tzu-Hui,et al."Diverse substrate recognition mechanism revealed by Thermotoga maritima Cel5A structures in complex with cellotetraose, cellobiose and mannotriose".BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS 1814.12(2011):1832-1840. |
入库方式： OAI收割
来源：天津工业生物技术研究所
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