6QE8

Crystal structure of Aspergillus niger GH11 endoxylanase XynA in complex with xylobiose epoxide activity based probe

6QE8 の概要

• エントリーDOI: 10.2210/pdb6qe8/pdb
• 分子名称: Endo-1,4-beta-xylanase A, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Aspergillus niger
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23894.32

構造登録者

Wu, L.,Rowland, R.J.,Davies, G.J. (登録日: 2019-01-07, 公開日: 2019-06-05, 最終更新日: 2024-01-24)

主引用文献

Schroder, S.P.,de Boer, C.,McGregor, N.G.S.,Rowland, R.J.,Moroz, O.,Blagova, E.,Reijngoud, J.,Arentshorst, M.,Osborn, D.,Morant, M.D.,Abbate, E.,Stringer, M.A.,Krogh, K.B.R.M.,Raich, L.,Rovira, C.,Berrin, J.G.,van Wezel, G.P.,Ram, A.F.J.,Florea, B.I.,van der Marel, G.A.,Codee, J.D.C.,Wilson, K.S.,Wu, L.,Davies, G.J.,Overkleeft, H.S.
Dynamic and Functional Profiling of Xylan-Degrading Enzymes inAspergillusSecretomes Using Activity-Based Probes.
Acs Cent.Sci., 5:1067-1078, 2019

PubMed Abstract: Plant polysaccharides represent a virtually unlimited feedstock for the generation of biofuels and other commodities. However, the extraordinary recalcitrance of plant polysaccharides toward breakdown necessitates a continued search for enzymes that degrade these materials efficiently under defined conditions. Activity-based protein profiling provides a route for the functional discovery of such enzymes in complex mixtures and under industrially relevant conditions. Here, we show the detection and identification of β-xylosidases and -β-1,4-xylanases in the secretomes of , by the use of chemical probes inspired by the β-glucosidase inhibitor cyclophellitol. Furthermore, we demonstrate the use of these activity-based probes (ABPs) to assess enzyme-substrate specificities, thermal stabilities, and other biotechnologically relevant parameters. Our experiments highlight the utility of ABPs as promising tools for the discovery of relevant enzymes useful for biomass breakdown.

PubMed: 31263766
DOI: 10.1021/acscentsci.9b00221

実験手法

X-RAY DIFFRACTION (1.79 Å)