5IJU

Structure of an AA10 Lytic Polysaccharide Monooxygenase from Bacillus amyloliquefaciens with Cu(II) bound

5IJU の概要

• エントリーDOI: 10.2210/pdb5iju/pdb
• 関連するPDBエントリー: 2yow 2yox 2yoy
• 分子名称: BaAA10 Lytic Polysaccharide Monooxygenase, COPPER (II) ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: lytic polysaccharide monooxygenase, copper ii, cazy aa10, oxidoreductase
• 由来する生物種: Bacillus amyloliquefaciens
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39985.35

構造登録者

Gregory, R.C.,Hemsworth, G.R.,Turkenburg, J.P.,Hart, S.J.,Walton, P.H.,Davies, G.J. (登録日: 2016-03-02, 公開日: 2016-09-21, 最終更新日: 2024-01-10)

主引用文献

Gregory, R.C.,Hemsworth, G.R.,Turkenburg, J.P.,Hart, S.J.,Walton, P.H.,Davies, G.J.
Activity, stability and 3-D structure of the Cu(ii) form of a chitin-active lytic polysaccharide monooxygenase from Bacillus amyloliquefaciens.
Dalton Trans, 45:16904-16912, 2016

PubMed Abstract: The enzymatic deconstruction of recalcitrant polysaccharide biomass is central to the conversion of these substrates for societal benefit, such as in biofuels. Traditional models for enzyme-catalysed polysaccharide degradation involved the synergistic action of endo-, exo- and processive glycoside hydrolases working in concert to hydrolyse the substrate. More recently this model has been succeeded by one featuring a newly discovered class of mononuclear copper enzymes: lytic polysaccharide monooxygenases (LPMOs; classified as Auxiliary Activity (AA) enzymes in the CAZy classification). In 2013, the structure of an LPMO from Bacillus amyloliquefaciens, BaAA10, was solved with the Cu centre photoreduced to Cu(i) in the X-ray beam. Here we present the catalytic activity of BaAA10. We show that it is a chitin-active LPMO, active on both α and β chitin, with the Cu(ii) binding with low nM K, and the substrate greatly increasing the thermal stability of the enzyme. A spiral data collection strategy has been used to facilitate access to the previously unobservable Cu(ii) state of the active centre, revealing a coordination geometry around the copper which is distorted from axial symmetry, consistent with the previous findings from EPR spectroscopy.

PubMed: 27722375
DOI: 10.1039/c6dt02793h

実験手法

X-RAY DIFFRACTION (1.7 Å)