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TitlepH- and concentration-dependent supramolecular assembly of a fungal defensin plectasin variant into helical non-amyloid fibrils.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 3162, Year 2022
Publish dateJun 7, 2022
AuthorsChristin 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 AbstractSelf-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.
External linksNat Commun / PubMed:35672293 / PubMed Central
MethodsEM (helical sym.) / X-ray diffraction
Resolution1.131 - 3.4 Å
Structure data

12775

7oae

EMDB-12775, PDB-7oae:
Cryo-EM structure of the plectasin fibril (double strands)
Method: EM (helical sym.) / Resolution: 2.0 Å

12776

7oag

EMDB-12776, PDB-7oag:
Cryo-EM structure of the plectasin fibril (single strand)
Method: EM (helical sym.) / Resolution: 3.4 Å

PDB-7o76:
Reversible supramolecular assembly of the anti-microbial peptide plectasin
Method: X-RAY DIFFRACTION / Resolution: 1.131 Å

Chemicals

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER / Diethylene glycol

ChemComp-HOH:
WATER / Water

Source
  • pseudoplectania nigrella (fungus)
KeywordsANTIMICROBIAL PROTEIN / fungal defensin / fibril / helical

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