4EIR

Structural basis for substrate targeting and catalysis by fungal polysaccharide monooxygenases (PMO-2)

4EIR の概要

• エントリーDOI: 10.2210/pdb4eir/pdb
• 関連するPDBエントリー: 4EIS
• 分子名称: polysaccharide monooxygenase-2, COPPER (II) ION, OXYGEN MOLECULE, ... (6 entities in total)
• 機能のキーワード: gh61, polysaccharide monooxygenase, pmo, cellulase, biofuels, cbm33, copper monooxygenase, peroxide, superoxide, cbp21, beta-sandwich fold, secreted, oxidoreductase
• 由来する生物種: Neurospora crassa
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47409.94

構造登録者

Li, X.,Beeson, W.T.,Phillips, C.M.,Marletta, M.A.,Cate, J.H. (登録日: 2012-04-05, 公開日: 2012-05-23, 最終更新日: 2023-09-13)

主引用文献

Li, X.,Beeson, W.T.,Phillips, C.M.,Marletta, M.A.,Cate, J.H.
Structural basis for substrate targeting and catalysis by fungal polysaccharide monooxygenases.
Structure, 20:1051-1061, 2012

PubMed Abstract: The use of cellulases remains a major cost in the production of renewable fuels and chemicals from lignocellulosic biomass. Fungi secrete copper-dependent polysaccharide monooxygenases (PMOs) that oxidatively cleave crystalline cellulose and improve the effectiveness of cellulases. However, the means by which PMOs recognize and cleave their substrates in the plant cell wall remain unclear. Here, we present structures of Neurospora crassa PMO-2 and PMO-3 at 1.10 and 1.37 Å resolution, respectively. In the structures, dioxygen species are found in the active sites, consistent with the proposed cleavage mechanism. Structural and sequence comparisons between PMOs also reveal that the enzyme substrate-binding surfaces contain highly varied aromatic amino acid and glycosylation positions. The structures reported here provide evidence for a wide range of PMO substrate recognition patterns in the plant cell wall, including binding modes that traverse multiple glucan chains.

PubMed: 22578542
DOI: 10.1016/j.str.2012.04.002

実験手法

X-RAY DIFFRACTION (1.1 Å)