7O76
Reversible supramolecular assembly of the anti-microbial peptide plectasin
This is a non-PDB format compatible entry.
Summary for 7O76
| Entry DOI | 10.2210/pdb7o76/pdb |
| Descriptor | Fungal defensin plectasin, DI(HYDROXYETHYL)ETHER (3 entities in total) |
| Functional Keywords | fungal defensin, antimicrobial protein |
| Biological source | Pseudoplectania nigrella (Ebony cup) |
| Total number of polymer chains | 1 |
| Total formula weight | 4521.14 |
| Authors | Pohl, C.,Noergaard, N.,Harris, P. (deposition date: 2021-04-13, release date: 2022-06-29, Last modification date: 2024-11-20) |
| Primary citation | Pohl, C.,Effantin, G.,Kandiah, E.,Meier, S.,Zeng, G.,Streicher, W.,Segura, D.R.,Mygind, P.H.,Sandvang, D.,Nielsen, L.A.,Peters, G.H.J.,Schoehn, G.,Mueller-Dieckmann, C.,Noergaard, A.,Harris, P. pH- and concentration-dependent supramolecular assembly of a fungal defensin plectasin variant into helical non-amyloid fibrils. Nat Commun, 13:3162-3162, 2022 Cited by PubMed Abstract: Self-assembly and fibril formation play important roles in protein behaviour. Amyloid fibril formation is well-studied due to its role in neurodegenerative diseases and characterized by refolding of the protein into predominantly β-sheet form. However, much less is known about the assembly of proteins into other types of supramolecular structures. Using cryo-electron microscopy at a resolution of 1.97 Å, we show that a triple-mutant of the anti-microbial peptide plectasin, PPI42, assembles into helical non-amyloid fibrils. The in vitro anti-microbial activity was determined and shown to be enhanced compared to the wildtype. Plectasin contains a cysteine-stabilised α-helix-β-sheet structure, which remains intact upon fibril formation. Two protofilaments form a right-handed protein fibril. The fibril formation is reversible and follows sigmoidal kinetics with a pH- and concentration dependent equilibrium between soluble monomer and protein fibril. This high-resolution structure reveals that α/β proteins can natively assemble into fibrils. PubMed: 35672293DOI: 10.1038/s41467-022-30462-w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.131 Å) |
Structure validation
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