6QE8
Crystal structure of Aspergillus niger GH11 endoxylanase XynA in complex with xylobiose epoxide activity based probe
Summary for 6QE8
Entry DOI | 10.2210/pdb6qe8/pdb |
Descriptor | Endo-1,4-beta-xylanase A, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, SULFATE ION, ... (5 entities in total) |
Functional Keywords | hydrolase |
Biological source | Aspergillus niger |
Total number of polymer chains | 1 |
Total formula weight | 23894.32 |
Authors | Wu, L.,Rowland, R.J.,Davies, G.J. (deposition date: 2019-01-07, release date: 2019-06-05, Last modification date: 2024-01-24) |
Primary citation | 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 Cited by 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: 31263766DOI: 10.1021/acscentsci.9b00221 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.79 Å) |
Structure validation
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