5N04
X-ray crystal structure of an LPMO
5N04 の概要
| エントリーDOI | 10.2210/pdb5n04/pdb |
| 分子名称 | Auxiliary activity 9, COPPER (II) ION, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| 機能のキーワード | lentinus similis lpmo aa9, lentinus similis lpmo, oxidoreductase |
| 由来する生物種 | Lentinus similis |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 25970.58 |
| 構造登録者 | Frandsen, K.E.H.,Poulsen, J.-C.N.,Lo Leggio, L. (登録日: 2017-02-02, 公開日: 2017-03-29, 最終更新日: 2024-01-17) |
| 主引用文献 | Frandsen, K.E.H.,Poulsen, J.N.,Tandrup, T.,Lo Leggio, L. Unliganded and substrate bound structures of the cellooligosaccharide active lytic polysaccharide monooxygenase LsAA9A at low pH. Carbohydr. Res., 448:187-190, 2017 Cited by PubMed Abstract: Lytic polysaccharide monooxygenases (LPMOs) have been found to be key components in microbial (bacterial and fungal) degradation of biomass. They are copper metalloenzymes that degrade polysaccharides oxidatively and act in synergy with glycoside hydrolases. Recently crystallographic studies carried out at pH 5.5 of the LPMO from Lentinus similis belonging to the fungal LPMO family AA9 have provided the first atomic resolution view of substrate-LPMO interactions. The LsAA9A structure presented here determined at pH 3.5 shows significant disorder of the active site in the absence of substrate ligand. Furthermore some differences are also observed in regards to substrate (cellohexaose) binding, although the major interaction with the N-terminal histidine remains unchanged. PubMed: 28364950DOI: 10.1016/j.carres.2017.03.010 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.76 Å) |
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