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3ZUD

THERMOASCUS GH61 ISOZYME A

3ZUD の概要
エントリーDOI10.2210/pdb3zud/pdb
関連するPDBエントリー2YET
分子名称GH61 ISOZYME A, COPPER (II) ION, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
機能のキーワードhydrolase, degradation of recalcitrant biomass
由来する生物種THERMOASCUS AURANTIACUS
タンパク質・核酸の鎖数1
化学式量合計25205.34
構造登録者
主引用文献Quinlan, R.J.,Sweeney, M.D.,Lo Leggio, L.,Otten, H.,Poulsen, J.-C.N.,Johansen, K.S.,Krogh, K.B.R.M.,Jorgensen, C.I.,Tovborg, M.,Anthonsen, A.,Tryfona, T.,Walter, C.P.,Dupree, P.,Xu, F.,Davies, G.J.,Walton, P.H.
Insights Into the Oxidative Degradation of Cellulose by a Copper Metalloenzyme that Exploits Biomass Components.
Proc.Natl.Acad.Sci.USA, 108:15079-, 2011
Cited by
PubMed Abstract: The enzymatic degradation of recalcitrant plant biomass is one of the key industrial challenges of the 21st century. Accordingly, there is a continuing drive to discover new routes to promote polysaccharide degradation. Perhaps the most promising approach involves the application of "cellulase-enhancing factors," such as those from the glycoside hydrolase (CAZy) GH61 family. Here we show that GH61 enzymes are a unique family of copper-dependent oxidases. We demonstrate that copper is needed for GH61 maximal activity and that the formation of cellodextrin and oxidized cellodextrin products by GH61 is enhanced in the presence of small molecule redox-active cofactors such as ascorbate and gallate. By using electron paramagnetic resonance spectroscopy and single-crystal X-ray diffraction, the active site of GH61 is revealed to contain a type II copper and, uniquely, a methylated histidine in the copper's coordination sphere, thus providing an innovative paradigm in bioinorganic enzymatic catalysis.
PubMed: 21876164
DOI: 10.1073/PNAS.1105776108
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.25 Å)
構造検証レポート
Validation report summary of 3zud
検証レポート(詳細版)ダウンロードをダウンロード

227561

件を2024-11-20に公開中

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