9IID
Crystal structure of PgAfp
Summary for 9IID
| Entry DOI | 10.2210/pdb9iid/pdb |
| Descriptor | Antifungal protein B (2 entities in total) |
| Functional Keywords | pgafp, antimicrobial protein |
| Biological source | Penicillium chrysogenum |
| Total number of polymer chains | 1 |
| Total formula weight | 6670.56 |
| Authors | Wang, Y. (deposition date: 2024-06-20, release date: 2024-07-10, Last modification date: 2025-05-21) |
| Primary citation | Wang, Y.,Wang, S.,Chen, Y.,Xie, C.,Xu, H.,Lin, Y.,Lin, R.,Zeng, W.,Chen, X.,Nie, X.,Wang, S. The role of Npt1 in regulating antifungal protein activity in filamentous fungi. Nat Commun, 16:2850-2850, 2025 Cited by PubMed Abstract: Pathogenic filamentous fungi pose a significant threat to global food security and human health. The limitations of available antifungal agents, including resistance and toxicity, highlight the need for developing innovative antifungal strategies. Antifungal proteins (AFPs) are a class of secreted small proteins that exhibit potent antifungal activity against filamentous fungi, yet the underlying mechanism remains partially understood. In this study, we investigate the molecular and cellular effects of two AFPs, PgAFP and AfAFP, on Aspergillus flavus, a representative filamentous fungus. These AFPs affect various fungal phenotypes and exert an intracellular effect by interacting with Ntp1, a fungi exclusive protein modulating diverse fungal traits. We find that Ntp1 amino acids 417-588 are critical for AFP binding and play a role in regulating growth, development, sporulation, sclerotia formation, toxin synthesis, and pathogenicity. Results generated from this study will help to control pathogenic fungi. PubMed: 40122888DOI: 10.1038/s41467-025-58230-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.78 Å) |
Structure validation
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