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Pohl, Christin; Effantin, Gregory; Kandiah, Eaazhisai; Meier, Sebastian; Zeng, Guanghong; Streicher, Werner; Segura, Dorotea Raventos; Mygind, Per H; Sandvang, Dorthe; Nielsen, Line Anker; Peters, Günther H J; Schoehn, Guy; Mueller-Dieckmann, Christoph; Noergaard, Allan; Harris, Pernille
Nature communications, 06/2022, Letnik: 13, Številka: 1Journal Article
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.
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in: SICRIS
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