8GF3
Crystallographic structure from BlMan5_7
8GF3 の概要
| エントリーDOI | 10.2210/pdb8gf3/pdb |
| 分子名称 | GH5 Mannanase, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, 1,2-ETHANEDIOL, ... (5 entities in total) |
| 機能のキーワード | mannanase, gh5, glycosil hydrolase, hydrolase |
| 由来する生物種 | Bacillus licheniformis |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 42788.42 |
| 構造登録者 | |
| 主引用文献 | Briganti, L.,Manzine, L.R.,de Mello Capetti, C.C.,de Araujo, E.A.,de Oliveira Arnoldi Pellegrini, V.,Guimaraes, F.E.G.,de Oliveira Neto, M.,Polikarpov, I. Unravelling biochemical and structural features of Bacillus licheniformis GH5 mannanase using site-directed mutagenesis and high-resolution protein crystallography studies. Int.J.Biol.Macromol., 274:133182-133182, 2024 Cited by PubMed Abstract: Glycoside hydrolase family 5 (GH5) encompasses enzymes with several different activities, including endo-1,4-β-mannosidases. These enzymes are involved in mannan degradation, and have a number of biotechnological applications, such as mannooligosaccharide prebiotics production, stain removal and dyes decolorization, to name a few. Despite the importance of GH5 enzymes, only a few members of subfamily 7 were structurally characterized. In the present work, biochemical and structural characterization of Bacillus licheniformis GH5 mannanase, BlMan5_7 were performed and the enzyme cleavage pattern was analyzed, showing that BlMan5_7 requires at least 5 occupied subsites to perform efficient hydrolysis. Additionally, crystallographic structure at 1.3 Å resolution was determined and mannoheptaose (M7) was docked into the active site to investigate the interactions between substrate and enzyme through molecular dynamic (MD) simulations, revealing the existence of a - 4 subsite, which might explain the generation of mannotetraose (M4) as an enzyme product. Biotechnological application of the enzyme in stain removal was investigated, demonstrating that BlMan5_7 addition to washing solution greatly improves mannan-based stain elimination. PubMed: 38885857DOI: 10.1016/j.ijbiomac.2024.133182 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.3 Å) |
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