3OM5
Crystal structure of B. megaterium levansucrase mutant N252A
3OM5 の概要
| エントリーDOI | 10.2210/pdb3om5/pdb |
| 関連するPDBエントリー | 3OM2 3OM4 3OM6 3OM7 |
| 分子名称 | Levansucrase, CALCIUM ION, HEXAETHYLENE GLYCOL, ... (7 entities in total) |
| 機能のキーワード | five fold beta-propeller, levansucrase, transferase |
| 由来する生物種 | Bacillus megaterium |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 205837.39 |
| 構造登録者 | Strube, C.P.,Homann, A.,Gamer, M.,Jahn, D.,Seibel, J.,Heinz, D.W. (登録日: 2010-08-26, 公開日: 2011-03-23, 最終更新日: 2024-02-21) |
| 主引用文献 | Strube, C.P.,Homann, A.,Gamer, M.,Jahn, D.,Seibel, J.,Heinz, D.W. Polysaccharide Synthesis of the Levansucrase SacB from Bacillus megaterium Is Controlled by Distinct Surface Motifs. J.Biol.Chem., 286:17593-17600, 2011 Cited by PubMed Abstract: Despite the widespread biological function of carbohydrates, the polysaccharide synthesis mechanisms of glycosyltransferases remain largely unexplored. Bacterial levansucrases (glycoside hydrolase family 68) synthesize high molecular weight, β-(2,6)-linked levan from sucrose by transfer of fructosyl units. The kinetic and biochemical characterization of Bacillus megaterium levansucrase SacB variants Y247A, Y247W, N252A, D257A, and K373A reveal novel surface motifs remote from the sucrose binding site with distinct influence on the polysaccharide product spectrum. The wild type activity (k(cat)) and substrate affinity (K(m)) are maintained. The structures of the SacB variants reveal clearly distinguishable subsites for polysaccharide synthesis as well as an intact active site architecture. These results lead to a new understanding of polysaccharide synthesis mechanisms. The identified surface motifs are discussed in the context of related glycosyltransferases. PubMed: 21454585DOI: 10.1074/jbc.M110.203166 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.95 Å) |
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