1UHV
Crystal structure of beta-D-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase
1UHV の概要
| エントリーDOI | 10.2210/pdb1uhv/pdb |
| 関連するPDBエントリー | 1PX8 |
| 分子名称 | Beta-xylosidase, 1,5-anhydro-2-deoxy-2-fluoro-D-xylitol (3 entities in total) |
| 機能のキーワード | family 39 glycoside hydrolase, xylosidase, xylan, xylose, covalent glycosyl-enzyme intermediate, hydrolase |
| 由来する生物種 | Thermoanaerobacterium saccharolyticum |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 235501.21 |
| 構造登録者 | Yang, J.K.,Yoon, H.J.,Ahn, H.J.,Il Lee, B.,Pedelacq, J.D.,Liong, E.C.,Berendzen, J.,Laivenieks, M.,Vieille, C.,Zeikus, G.J.,Vocadlo, D.J.,Withers, S.G.,Suh, S.W. (登録日: 2003-07-11, 公開日: 2003-12-23, 最終更新日: 2024-11-06) |
| 主引用文献 | Yang, J.K.,Yoon, H.J.,Ahn, H.J.,Lee, B.I.,Pedelacq, J.D.,Liong, E.C.,Berendzen, J.,Laivenieks, M.,Vieille, C.,Zeikus, G.J.,Vocadlo, D.J.,Withers, S.G.,Suh, S.W. Crystal structure of beta-D-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase. J.Mol.Biol., 335:155-165, 2004 Cited by PubMed Abstract: 1,4-beta-D-Xylan is the major component of plant cell-wall hemicelluloses. beta-D-Xylosidases are involved in the breakdown of xylans into xylose and belong to families 3, 39, 43, 52, and 54 of glycoside hydrolases. Here, we report the first crystal structure of a member of family 39 glycoside hydrolase, i.e. beta-D-xylosidase from Thermoanaerobacterium saccharolyticum strain B6A-RI. This study also represents the first structure of any beta-xylosidase of the above five glycoside hydrolase families. Each monomer of T. saccharolyticum beta-xylosidase comprises three distinct domains; a catalytic domain of the canonical (beta/alpha)(8)-barrel fold, a beta-sandwich domain, and a small alpha-helical domain. We have determined the structure in two forms: D-xylose-bound enzyme and a covalent 2-deoxy-2-fluoro-alpha-D-xylosyl-enzyme intermediate complex, thus providing two snapshots in the reaction pathway. This study provides structural evidence for the proposed double displacement mechanism that involves a covalent intermediate. Furthermore, it reveals possible functional roles for His228 as the auxiliary acid/base and Glu323 as a key residue in substrate recognition. PubMed: 14659747DOI: 10.1016/j.jmb.2003.10.026 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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