1PT2
Crystal structure of levansucrase (E342A) complexed with sucrose
1PT2 の概要
| エントリーDOI | 10.2210/pdb1pt2/pdb |
| 関連するPDBエントリー | 1OYG |
| 関連するBIRD辞書のPRD_ID | PRD_900003 |
| 分子名称 | Levansucrase, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, CALCIUM ION, ... (4 entities in total) |
| 機能のキーワード | glycoside hydrolase, levansucrase, beta-propeller, levan, sucrose, transferase |
| 由来する生物種 | Bacillus subtilis |
| 細胞内の位置 | Secreted: P05655 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 50646.96 |
| 構造登録者 | |
| 主引用文献 | Meng, G.,Futterer, K. Structural framework of fructosyl transfer in Bacillus subtilis levansucrase Nat.Struct.Biol., 10:935-941, 2003 Cited by PubMed Abstract: Many bacteria and about 40,000 plant species form primary carbohydrate reserves based on fructan; these polymers of beta-D-fructofuranose are thought to confer tolerance to drought and frost in plants. Microbial fructan, the beta(2,6)-linked levan, is synthesized directly from sucrose by levansucrase, which is able to catalyze both sucrose hydrolysis and levan polymerization. The crystal structure of Bacillus subtilis levansucrase, determined to a resolution of 1.5 A, shows a rare five-fold beta-propeller topology with a deep, negatively charged central pocket. Arg360, a residue essential for polymerase activity, lies in a solvent-exposed site adjacent to the central pocket. Mutagenesis data and the sucrose-bound structure of inactive levansucrase E342A, at a resolution of 2.1 A, strongly suggest that three conserved acidic side chains in the central pocket are critical for catalysis, and presumably function as nucleophile (Asp86) and general acid (Glu342), or stabilize the transition state (Asp247). PubMed: 14517548DOI: 10.1038/nsb974 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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