8HE4

The structure of chitin deacetylase Pst_13661 from Puccinia striiformis f. sp. tritici

Summary for 8HE4

• Entry DOI: 10.2210/pdb8he4/pdb
• Descriptor: Chitin deacetylase, ZINC ION, ~{N}-oxidanylnaphthalene-1-carboxamide, ... (4 entities in total)
• Functional Keywords: chitin deacetylase, plant pathogenic fungi, virulence factor, hydrolase
• Biological source: Puccinia striiformis f. sp. tritici
• Total number of polymer chains: 1
• Total formula weight: 31888.99

Authors

Liu, L.,Li, Y.C.,Zhou, Y.,Yang, Q. (deposition date: 2022-11-07, release date: 2023-05-31, Last modification date: 2024-10-23)

Primary citation

Liu, L.,Xia, Y.,Li, Y.,Zhou, Y.,Su, X.,Yan, X.,Wang, Y.,Liu, W.,Cheng, H.,Wang, Y.,Yang, Q.
Inhibition of chitin deacetylases to attenuate plant fungal diseases.
Nat Commun, 14:3857-3857, 2023

PubMed Abstract: 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.

PubMed: 37385996
DOI: 10.1038/s41467-023-39562-7

Experimental method

X-RAY DIFFRACTION (1.93 Å)