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<StructureSection load='6q8m' size='340' side='right'caption='[[6q8m]], [[Resolution|resolution]] 1.42&Aring;' scene=''>
<StructureSection load='6q8m' size='340' side='right'caption='[[6q8m]], [[Resolution|resolution]] 1.42&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6q8m]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q8M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q8M FirstGlance]. <br>
<table><tr><td colspan='2'>[[6q8m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_aculeatus_ATCC_16872 Aspergillus aculeatus ATCC 16872]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q8M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Q8M FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.42&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6q8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q8m OCA], [http://pdbe.org/6q8m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q8m RCSB], [http://www.ebi.ac.uk/pdbsum/6q8m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q8m ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6q8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q8m OCA], [https://pdbe.org/6q8m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6q8m RCSB], [https://www.ebi.ac.uk/pdbsum/6q8m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6q8m ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1L9WG58_ASPA1 A0A1L9WG58_ASPA1]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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 beta-xylosidases and endo-beta-1,4-xylanases in the secretomes of Aspergillus niger, by the use of chemical probes inspired by the beta-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.
Dynamic and Functional Profiling of Xylan-Degrading Enzymes in Aspergillus Secretomes Using Activity-Based Probes.,Schroder SP, de Boer C, McGregor NGS, Rowland RJ, Moroz O, Blagova E, Reijngoud J, Arentshorst M, Osborn D, Morant MD, Abbate E, Stringer MA, Krogh KBRM, Raich L, Rovira C, Berrin JG, van Wezel GP, Ram AFJ, Florea BI, van der Marel GA, Codee JDC, Wilson KS, Wu L, Davies GJ, Overkleeft HS ACS Cent Sci. 2019 Jun 26;5(6):1067-1078. doi: 10.1021/acscentsci.9b00221. Epub, 2019 May 24. PMID:31263766<ref>PMID:31263766</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6q8m" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Endo-1,4-beta-xylanase]]
[[Category: Aspergillus aculeatus ATCC 16872]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Blagova, E]]
[[Category: Blagova E]]
[[Category: Davies, G J]]
[[Category: Davies GJ]]
[[Category: Moroz, O]]
[[Category: Moroz O]]
[[Category: Rowland, R J]]
[[Category: Rowland RJ]]
[[Category: Wu, L]]
[[Category: Wu L]]
[[Category: Hydrolase]]

Latest revision as of 13:02, 6 November 2024

GH10 endo-xylanase

6q8m, resolution 1.42Å

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