5JRM
Crystal Structure of a Xylanase at 1.56 Angstroem resolution
5JRM の概要
| エントリーDOI | 10.2210/pdb5jrm/pdb |
| 分子名称 | Endo-1,4-beta-xylanase, GLYCEROL, SULFATE ION, ... (4 entities in total) |
| 機能のキーワード | xylanase, gh11, hydrolase |
| 由来する生物種 | Fusarium oxysporum |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 21625.33 |
| 構造登録者 | Gomez, S.,Payne, A.M.,Savko, M.,Fox, G.C.,Shepard, W.E.,Fernandez, F.J.,Vega, M.C. (登録日: 2016-05-06, 公開日: 2017-05-24, 最終更新日: 2024-10-23) |
| 主引用文献 | Gomez, S.,Payne, A.M.,Savko, M.,Fox, G.C.,Shepard, W.E.,Fernandez, F.J.,Cristina Vega, M. Structural and functional characterization of a highly stable endo-beta-1,4-xylanase from Fusarium oxysporum and its development as an efficient immobilized biocatalyst. Biotechnol Biofuels, 9:191-191, 2016 Cited by PubMed Abstract: Replacing fossil fuel with renewable sources such as lignocellulosic biomass is currently a promising alternative for obtaining biofuel and for fighting against the consequences of climate change. However, the recalcitrant structure of lignocellulosic biomass residues constitutes a major limitation for its widespread use in industry. The efficient hydrolysis of lignocellulosic materials requires the complementary action of multiple enzymes including xylanases and β-xylosidases, which are responsible for cleaving exo- and endoxylan linkages, that release oligocarbohydrates that can be further processed by other enzymes. PubMed: 27602054DOI: 10.1186/s13068-016-0605-z 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.56 Å) |
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