6SD0
Structure of beta-galactosidase from Thermotoga maritima.
6SD0 の概要
| エントリーDOI | 10.2210/pdb6sd0/pdb |
| 分子名称 | Beta-galactosidase, MAGNESIUM ION (3 entities in total) |
| 機能のキーワード | beta-galactosidase, glycoside hydrolase, hydrolysis, galactooligosaccharide, thermotoga maritima, thermoresistant, lactose, glycosyl hydrolase 2 family. sugar binding protein, hydrolase |
| 由来する生物種 | Thermotoga maritima MSB8 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 511236.19 |
| 構造登録者 | Jimenez-Ortega, E.,Ramirez-Escudero, M.,Sanz-Aparicio, J. (登録日: 2019-07-26, 公開日: 2020-01-15, 最終更新日: 2024-01-24) |
| 主引用文献 | Miguez Amil, S.,Jimenez-Ortega, E.,Ramirez-Escudero, M.,Talens-Perales, D.,Marin-Navarro, J.,Polaina, J.,Sanz-Aparicio, J.,Fernandez-Leiro, R. The cryo-EM Structure ofThermotoga maritimabeta-Galactosidase: Quaternary Structure Guides Protein Engineering. Acs Chem.Biol., 15:179-188, 2020 Cited by PubMed Abstract: Lactose intolerance is a common digestive disorder that affects a large proportion of the adult human population. The severity of the symptoms is highly variable, depending on the susceptibility to the sugar and the amount digested. For that reason, enzymes that can be used for the production of lactose-free milk and milk derivatives have acquired singular biotechnological importance. One such case is β-galactosidase (TmLac). Here, we report the cryo-EM structure of TmLac at 2.0 Å resolution. The protein features a newly solved domain at its C-terminus, characteristic of the genus , which promotes a peculiar octameric arrangement. We have assessed the constraints imposed by the quaternary protein structure on the construction of hybrid versions of this GH2 enzyme. Carbohydrate binding modules (CBM) from the CBM2 and CBM9 families have been added at either the amino or carboxy terminus, and the structural and functional effects of such modifications have been analyzed. The results provide a basis for the rational design of hybrid enzymes that can be efficiently attached to different solid supports. PubMed: 31874027DOI: 10.1021/acschembio.9b00752 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.7 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






