6Q8M
GH10 endo-xylanase
Summary for 6Q8M
| Entry DOI | 10.2210/pdb6q8m/pdb |
| Descriptor | Beta-xylanase, 2-acetamido-2-deoxy-beta-D-glucopyranose, 1,2-ETHANEDIOL, ... (5 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Aspergillus aculeatus ATCC 16872 |
| Total number of polymer chains | 2 |
| Total formula weight | 89024.86 |
| Authors | Davies, G.J.,Rowland, R.J.,Wu, L.,Moroz, O.,Blagova, E. (deposition date: 2018-12-15, release date: 2019-06-05, Last modification date: 2024-11-06) |
| 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 (1.42 Å) |
Structure validation
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