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6QE8

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

Summary for 6QE8
Entry DOI10.2210/pdb6qe8/pdb
DescriptorEndo-1,4-beta-xylanase A, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, SULFATE ION, ... (5 entities in total)
Functional Keywordshydrolase
Biological sourceAspergillus niger
Total number of polymer chains1
Total formula weight23894.32
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 citationSchroder, 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: 31263766
DOI: 10.1021/acscentsci.9b00221
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.79 Å)
Structure validation

226707

数据于2024-10-30公开中

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