4MAH
Structure of Aspergillus oryzae AA11 Lytic Polysaccharide Monooxygenase with Zn
4MAH の概要
| エントリーDOI | 10.2210/pdb4mah/pdb |
| 関連するPDBエントリー | 4MAI |
| 分子名称 | AA11 Lytic Polysaccharide Monooxygenase, ZINC ION, 1,2-ETHANEDIOL, ... (5 entities in total) |
| 機能のキーワード | chitin oxidation, gh61, aa11, chitin degradation, oxidoreductase |
| 由来する生物種 | Aspergillus oryzae (Yellow koji mold) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 23240.77 |
| 構造登録者 | Hemsworth, G.R.,Henrissat, B.,Walton, P.H.,Davies, G.J. (登録日: 2013-08-16, 公開日: 2013-12-18, 最終更新日: 2024-11-20) |
| 主引用文献 | Hemsworth, G.R.,Henrissat, B.,Davies, G.J.,Walton, P.H. Discovery and characterization of a new family of lytic polysaccharide monooxygenases. Nat.Chem.Biol., 10:122-126, 2014 Cited by PubMed Abstract: Lytic polysaccharide monooxygenases (LPMOs) are a recently discovered class of enzymes capable of oxidizing recalcitrant polysaccharides. They are attracting considerable attention owing to their potential use in biomass conversion, notably in the production of biofuels. Previous studies have identified two discrete sequence-based families of these enzymes termed AA9 (formerly GH61) and AA10 (formerly CBM33). Here, we report the discovery of a third family of LPMOs. Using a chitin-degrading exemplar from Aspergillus oryzae, we show that the three-dimensional structure of the enzyme shares some features of the previous two classes of LPMOs, including a copper active center featuring the 'histidine brace' active site, but is distinct in terms of its active site details and its EPR spectroscopy. The newly characterized AA11 family expands the LPMO clan, potentially broadening both the range of potential substrates and the types of reactive copper-oxygen species formed at the active site of LPMOs. PubMed: 24362702DOI: 10.1038/nchembio.1417 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.55 Å) |
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