https://scholars.lib.ntu.edu.tw/handle/123456789/414378
標題: | Crystal structure of truncated Fibrobacter succinogenes 1,3-1,4-£]-D-glucanase in complex with £]-1,3-1,4-cellotriose | 作者: | Tsai L.-C. Shyur L.-F. Cheng Y.-S. Lee S.-H. |
關鍵字: | £]-1,3-1,4-cellotriose (CLTR);1,3-1,4-£]-D-glucanase;Active cleft;Glucanase | 公開日期: | 2005 | 卷: | 354 | 期: | 3 | 起(迄)頁: | 642-651 | 來源出版物: | Journal of Molecular Biology | 摘要: | Fibrobacter succinogenes 1,3-1,4-£]-d-glucanase (Fs£]-glucanase) catalyzes the specific hydrolysis of £]-1,4 glycosidic bonds adjacent to £]-1,3 linkages in £]-d-glucans or lichenan. This is the first report to elucidate the crystal structure of a truncated Fs£]-glucanase (TFs£]-glucanase) in complex with £]-1,3-1,4-cellotriose, a major product of the enzyme reaction. The crystal structures, at a resolution of 2.3 ?, reveal that the overall fold of TFs£]-glucanase remains virtually unchanged upon sugar binding. The enzyme accommodates five glucose residues, forming a concave active cleft. The £]-1,3-1,4-cellotriose with subsites -3 to -1 bound to the active cleft of TFs£]-glucanase with its reducing end subsite -1 close to the key catalytic residues Glu56 and Glu60. All three subsites of the £]-1,3-1,4-cellotriose adopted a relaxed 4C 1 conformation, with a £]-1,3 glycosidic linkage between subsites -2 and -1, and a £]-1,4 glycosidic linkage between subsites -3 and -2. On the basis of the enzyme-product complex structure observed in this study, a catalytic mechanism and substrate binding conformation of the active site of TFs£]-glucanase is proposed. ? 2005 Elsevier Ltd. All rights reserved. |
URI: | https://scholars.lib.ntu.edu.tw/handle/123456789/414378 | ISSN: | 00222836 | DOI: | 10.1016/j.jmb.2005.09.041 |
顯示於: | 植物科學研究所 |
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