The substrate/product-binding modes of a novel GH120 beta-xylosidase (XylC) from Thermoanaerobacterium saccharolyticum JW/SL-YS485
文献类型：期刊论文
| 作者 | Huang, Chun-Hsiang2; Sun, Yu3; Ko, Tzu-Ping4; Chen, Chun-Chi5; Zheng, Yingying2; Chan, Hsiu-Chien2; Pang, Xuefei2; Wiegel, Juergen1; Shao, Weilan3; Guo, Rey-Ting2 |
| 刊名 | BIOCHEMICAL JOURNAL
 |
| 出版日期 | 2012-12-15 |
| 卷号 | 448页码:401-407 |
| 关键词 | crystal structure glycoside hydrolase synchrotron radiation Thermoanaerobacterium saccharolyticum xylan beta-xylosidase |
| 英文摘要 | Xylan-1,4-beta-xylosidase (beta-xylosidase) hydrolyses xylo-oligomers at their non-reducing ends into individual xylose units. Recently, XylC, a beta-xylosidase from Thermoanaerobacterium saccharolyticum JW/SL-YS485, was found to be structurally different from corresponding glycosyl hydrolases in the CAZy database (http://www.cazy.org/), and was subsequently classified as the first member of a novel family of glycoside hydrolases (GH120). In the present paper, we report three crystal structures of XylC in complex with Tris, xylobiose and xylose at 1.48-2.05 angstrom (1 angstrom = 0.1 nm) resolution. XylC assembles into a tetramer, and each monomer comprises two distinct domains. The core domain is a right-handed parallel beta-helix (residues 1-75 and 201-638) and the flanking region (residues 76-200) folds into a beta-sandwich domain. The enzyme contains an open carbohydrate-binding cleft, allowing accommodation of longer xylo-oligosaccharides. On the basis of the crystal structures and in agreement with previous kinetic data, we propose that XylC cleaves the glycosidic bond by the retaining mechanism using two acidic residues Asp(382) (nucleophile) and Glu(405) (general acid/base). In addition to the active site, nine other xylose-binding sites were consistently observed in each of the four monomers, providing a possible reason for the high tolerance of product inhibition. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biochemistry & Molecular Biology |
| 研究领域[WOS] | Biochemistry & Molecular Biology |
| 关键词[WOS] | PYROPHOSPHATE SYNTHASE ; DENSITY MODIFICATION ; STRAIN JW/SL-YS485 ; CRYSTAL-STRUCTURE ; ENZYME ; PURIFICATION ; REFINEMENT ; MECHANISM ; SOFTWARE ; XYLANASE |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000312230600010 |
| 源URL | [http://124.16.173.210/handle/834782/1308]  |
| 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.Univ Georgia, Dept Microbiol, Athens, GA 30602 USA 2.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Ind Enzymes Natl Engn Lab, Tianjin 300308, Peoples R China 3.Jiangsu Univ, Sch Environm, Biofuels Inst, Zhenjiang 212013, Peoples R China 4.Acad Sinica, Inst Biol Chem, Taipei 11529, Taiwan 5.Chinese Acad Sci, Inst Microbiol, CAS Key Lab Pathogen Microbiol & Immunol, Beijing 100101, Peoples R China |
| 推荐引用方式 GB/T 7714 | Huang, Chun-Hsiang,Sun, Yu,Ko, Tzu-Ping,et al. The substrate/product-binding modes of a novel GH120 beta-xylosidase (XylC) from Thermoanaerobacterium saccharolyticum JW/SL-YS485[J]. BIOCHEMICAL JOURNAL,2012,448:401-407. |
| APA | Huang, Chun-Hsiang.,Sun, Yu.,Ko, Tzu-Ping.,Chen, Chun-Chi.,Zheng, Yingying.,...&Guo, Rey-Ting.(2012).The substrate/product-binding modes of a novel GH120 beta-xylosidase (XylC) from Thermoanaerobacterium saccharolyticum JW/SL-YS485.BIOCHEMICAL JOURNAL,448,401-407. |
| MLA | Huang, Chun-Hsiang,et al."The substrate/product-binding modes of a novel GH120 beta-xylosidase (XylC) from Thermoanaerobacterium saccharolyticum JW/SL-YS485".BIOCHEMICAL JOURNAL 448(2012):401-407. |
入库方式： OAI收割
来源：天津工业生物技术研究所
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