6M0E
Beijerinckia indica beta-fructosyltransferase complexed with fructose
6M0E の概要
エントリーDOI | 10.2210/pdb6m0e/pdb |
分子名称 | Levansucrase, MAGNESIUM ION, beta-D-fructofuranose, ... (5 entities in total) |
機能のキーワード | gh68, fructooligosaccharide, hydrolase |
由来する生物種 | Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIB 8712) |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 57978.49 |
構造登録者 | |
主引用文献 | Tonozuka, T.,Kitamura, J.,Nagaya, M.,Kawai, R.,Nishikawa, A.,Hirano, K.,Tamura, K.,Fujii, T.,Tochio, T. Crystal structure of a glycoside hydrolase family 68 beta-fructosyltransferase from Beijerinckia indica subsp. indica in complex with fructose. Biosci.Biotechnol.Biochem., 84:2508-2520, 2020 Cited by PubMed Abstract: An enzyme belonging to glycoside hydrolase family 68 (GH68) from subsp. NBRC 3744 was expressed in . Biochemical characterization showed that the enzyme was identified to be a β-fructosyltransferase (BiBftA). Crystallization of a full-length BiBftA was initially attempted, but no crystals were obtained. We constructed a variant in which 5 residues (Pro199-Gly203) and 13 residues (Leu522-Gln534) in potentially flexible regions were deleted, and we successfully crystallized this variant BiBftA. BiBftA is composed of a five-bladed β-propeller fold as in other GH68 enzymes. The structure of BiBftA in complex with fructose unexpectedly indicated that one β-fructofuranose (β-Fru) molecule and one β-fructopyranose molecule bind to the catalytic pocket. The orientation of β-Fru at subsite -1 is tilted from the orientation observed in most GH68 enzymes, presenting a second structure of a GH68 enzyme in complex with the tilted binding mode of β-Fru PubMed: 32752982DOI: 10.1080/09168451.2020.1804317 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.35 Å) |
構造検証レポート
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