8he4
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8he4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Puccinia_striiformis_f._sp._tritici Puccinia striiformis f. sp. tritici]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HE4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HE4 FirstGlance]. <br> | <table><tr><td colspan='2'>[[8he4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Puccinia_striiformis_f._sp._tritici Puccinia striiformis f. sp. tritici]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HE4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HE4 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8GK:~{N}-oxidanylnaphthalene-1-carboxamide'>8GK</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.93Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8GK:~{N}-oxidanylnaphthalene-1-carboxamide'>8GK</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=8he4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8he4 OCA], [https://pdbe.org/8he4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8he4 RCSB], [https://www.ebi.ac.uk/pdbsum/8he4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8he4 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=8he4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8he4 OCA], [https://pdbe.org/8he4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8he4 RCSB], [https://www.ebi.ac.uk/pdbsum/8he4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8he4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [https://www.uniprot.org/uniprot/ | + | [https://www.uniprot.org/uniprot/A0A2S4W2W0_9BASI A0A2S4W2W0_9BASI] |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Phytopathogenic fungi secrete chitin deacetylase (CDA) to escape the host's immunological defense during infection. Here, we showed that the deacetylation activity of CDA toward chitin is essential for fungal virulence. Five crystal structures of two representative and phylogenetically distant phytopathogenic fungal CDAs, VdPDA1 from Verticillium dahliae and Pst_13661 from Puccinia striiformis f. sp. tritici, were obtained in ligand-free and inhibitor-bound forms. These structures suggested that both CDAs have an identical substrate-binding pocket and an Asp-His-His triad for coordinating a transition metal ion. Based on the structural identities, four compounds with a benzohydroxamic acid (BHA) moiety were obtained as phytopathogenic fungal CDA inhibitors. BHA exhibited high effectiveness in attenuating fungal diseases in wheat, soybean, and cotton. Our findings revealed that phytopathogenic fungal CDAs share common structural features, and provided BHA as a lead compound for the design of CDA inhibitors aimed at attenuating crop fungal diseases. | ||
| + | |||
| + | Inhibition of chitin deacetylases to attenuate plant fungal diseases.,Liu L, Xia Y, Li Y, Zhou Y, Su X, Yan X, Wang Y, Liu W, Cheng H, Wang Y, Yang Q Nat Commun. 2023 Jun 29;14(1):3857. doi: 10.1038/s41467-023-39562-7. PMID:37385996<ref>PMID:37385996</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8he4" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
The structure of chitin deacetylase Pst_13661 from Puccinia striiformis f. sp. tritici
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