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pH- and concentrati...
pH- and concentration-dependent supramolecular assembly of a fungal defensin plectasin variant into helical non-amyloid fibrils
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- Pohl, Christin (author)
- Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,LTH profilområde: Nanovetenskap och halvledarteknologi,LTH profilområden,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH,LTH Profile Area: Nanoscience and Semiconductor Technology,LTH Profile areas,Faculty of Engineering, LTH,Novozymes A/S,Technical University of Denmark
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- Effantin, Gregory (author)
- University Grenoble Alpes
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- Kandiah, Eaazhisai (author)
- European Synchrotron Radiation Facility
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- Meier, Sebastian (author)
- Technical University of Denmark
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- Zeng, Guanghong (author)
- Novo Nordisk A/S,Danish National Metrology Institute
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- Streicher, Werner (author)
- Novozymes A/S
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- Segura, Dorotea Raventos (author)
- Novozymes A/S
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- Mygind, Per H. (author)
- Novozymes A/S
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- Sandvang, Dorthe (author)
- Novozymes A/S
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- Nielsen, Line Anker (author)
- Novozymes A/S
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- Peters, Günther H.J. (author)
- Technical University of Denmark
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- Schoehn, Guy (author)
- University Grenoble Alpes
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- Mueller-Dieckmann, Christoph (author)
- European Synchrotron Radiation Facility
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- Noergaard, Allan (author)
- Novozymes A/S
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- Harris, Pernille (author)
- Technical University of Denmark,University of Copenhagen
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(creator_code:org_t)
- 2022-06-07
- 2022
- English.
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In: Nature Communications. - : Springer Science and Business Media LLC. - 2041-1723. ; 13:1
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Abstract
Subject headings
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- 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.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
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- ref (subject category)
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- By the author/editor
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Pohl, Christin
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Effantin, Gregor ...
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Kandiah, Eaazhis ...
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Meier, Sebastian
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Zeng, Guanghong
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Streicher, Werne ...
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show more...
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Segura, Dorotea ...
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Mygind, Per H.
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Sandvang, Dorthe
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Nielsen, Line An ...
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Peters, Günther ...
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Schoehn, Guy
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Mueller-Dieckman ...
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Noergaard, Allan
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Harris, Pernille
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- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Biochemistry and ...
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Nature Communica ...
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Lund University