+検索条件
-Structure paper
タイトル | pH- and concentration-dependent supramolecular assembly of a fungal defensin plectasin variant into helical non-amyloid fibrils. |
---|---|
ジャーナル・号・ページ | Nat Commun, Vol. 13, Issue 1, Page 3162, Year 2022 |
掲載日 | 2022年6月7日 |
著者 | Christin Pohl / Gregory Effantin / Eaazhisai Kandiah / Sebastian Meier / Guanghong Zeng / Werner Streicher / Dorotea Raventos Segura / Per H Mygind / Dorthe Sandvang / Line Anker Nielsen / Günther H J Peters / Guy Schoehn / Christoph Mueller-Dieckmann / Allan Noergaard / Pernille Harris / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:35672293 / PubMed Central |
手法 | EM (らせん対称) / X線回折 |
解像度 | 1.131 - 3.4 Å |
構造データ | EMDB-12775, PDB-7oae: EMDB-12776, PDB-7oag: PDB-7o76: |
化合物 | ChemComp-PEG: ChemComp-HOH: |
由来 |
|
キーワード | ANTIMICROBIAL PROTEIN / fungal defensin / fibril / helical |