5JRN
Crystal Structure of a Xylanase in Complex with a Monosaccharide at 2.84 Angstroem resolution
5JRN の概要
エントリーDOI | 10.2210/pdb5jrn/pdb |
分子名称 | Endo-1,4-beta-xylanase, GLYCEROL, methyl beta-D-xylopyranoside, ... (4 entities in total) |
機能のキーワード | xylanase, complex, gh11, hydrolase |
由来する生物種 | Fusarium oxysporum f. sp. vasinfectum 25433 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 22053.86 |
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 (2.841 Å) |
構造検証レポート
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