Crystal structure and substrate-binding mode of cellulase 12A from Thermotoga maritima
文献类型：期刊论文
| 作者 | Cheng, Ya-Shan1; Ko, Tzu-Ping2; Wu, Tzu-Hui3; Ma, Yanhe4; Huang, Chun-Hsiang5; Lai, Hui-Lin3; Wang, Andrew H. -J.2,5; Liu, Je-Ruei1,6; Guo, Rey-Ting4 |
| 刊名 | PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
 |
| 出版日期 | 2011-04-01 |
| 卷号 | 79期号:4页码:1193-1204 |
| 关键词 | hyperthermophile endoglucanase catalytic intermediate active site mutant mercury derivatives synchrotron radiations biofuel industry |
| 英文摘要 | Cellulases have been used in many applications to treat various carbohydrate-containing materials. Thermotoga maritima cellulase 12A (TmCel12A) belongs to the GH12 family of glycoside hydrolases. It is a beta-1,4-endoglucanase that degrades cellulose molecules into smaller fragments, facilitating further utilization of the carbohydrate. Because of its hyperthermophilic nature, the enzyme is especially suitable for industrial applications. Here the crystal structure of TmCel12A was determined by using an active-site mutant E134C and its mercury-containing derivatives. It adopts a beta-jellyroll protein fold typical of the GH12-family enzymes, with two curved beta-sheets A and B and a central active-site cleft. Structural comparison with other GH12 enzymes shows significant differences, as found in two longer and highly twisted beta-strands B8 and B9 and several loops. A unique Loop A3-B3 that contains Arg60 and Tyr61 stabilizes the substrate by hydrogen bonding and stacking, as observed in the complex crystals with cellotetraose and cellobiose. The high-resolution structures allow clear elucidation of the network of interactions between the enzyme and its substrate. The sugar residues bound to the enzyme appear to be more ordered in the -2 and -1 subsites than in the +1, +2 and -3 subsites. In the E134C crystals the bound -1 sugar at the cleavage site consistently show the alpha-anomeric configuration, implicating an intermediate-like structure. |
| 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] | 1.2 ANGSTROM RESOLUTION ; X-RAY ; THERMAL-STABILITY ; ENDOGLUCANASE ; CEL12A ; DIFFRACTION ; COMPLEX ; ENZYMES ; SYSTEM |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000288138700013 |
| 公开日期 | 2014-12-24 |
| 源URL | [http://124.16.173.210/handle/311007/561]  |
| 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.Acad Sinica, Inst Biol Chem, Taipei 115, Taiwan 3.Genozyme Biotechnol Inc, Taipei 106, Taiwan 4.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Tianjin 300308, Peoples R China 5.Acad Sinica, Genom Res Ctr, Taipei 115, Taiwan 6.Natl Taiwan Univ, Dept Anim Sci & Technol, Taipei 106, Taiwan |
| 推荐引用方式 GB/T 7714 | Cheng, Ya-Shan,Ko, Tzu-Ping,Wu, Tzu-Hui,et al. Crystal structure and substrate-binding mode of cellulase 12A from Thermotoga maritima[J]. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS,2011,79(4):1193-1204. |
| APA | Cheng, Ya-Shan.,Ko, Tzu-Ping.,Wu, Tzu-Hui.,Ma, Yanhe.,Huang, Chun-Hsiang.,...&Guo, Rey-Ting.(2011).Crystal structure and substrate-binding mode of cellulase 12A from Thermotoga maritima.PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS,79(4),1193-1204. |
| MLA | Cheng, Ya-Shan,et al."Crystal structure and substrate-binding mode of cellulase 12A from Thermotoga maritima".PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS 79.4(2011):1193-1204. |
入库方式： OAI收割
来源：天津工业生物技术研究所
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