6G8C
Crystal Structure of the Amyloid-like IYQYGG segment from the R1 repeat of the E. coli Biofilm-associated CsgA Curli protein
Summary for 6G8C
| Entry DOI | 10.2210/pdb6g8c/pdb |
| Descriptor | Major curlin subunit (2 entities in total) |
| Functional Keywords | bacterial steric-zipper cross-beta amyloid fibril from e. coli, protein fibril |
| Biological source | Escherichia coli K-12 |
| Total number of polymer chains | 1 |
| Total formula weight | 699.75 |
| Authors | Landau, M.,Perov, S. (deposition date: 2018-04-08, release date: 2019-04-24, Last modification date: 2024-05-01) |
| Primary citation | Perov, S.,Lidor, O.,Salinas, N.,Golan, N.,Tayeb-Fligelman, E.,Deshmukh, M.,Willbold, D.,Landau, M. Structural Insights into Curli CsgA Cross-beta Fibril Architecture Inspire Repurposing of Anti-amyloid Compounds as Anti-biofilm Agents. Plos Pathog., 15:e1007978-e1007978, 2019 Cited by PubMed Abstract: Curli amyloid fibrils secreted by Enterobacteriaceae mediate host cell adhesion and contribute to biofilm formation, thereby promoting bacterial resistance to environmental stressors. Here, we present crystal structures of amyloid-forming segments from the major curli subunit, CsgA, revealing steric zipper fibrils of tightly mated β-sheets, demonstrating a structural link between curli and human pathological amyloids. D-enantiomeric peptides, originally developed to interfere with Alzheimer's disease-associated amyloid-β, inhibited CsgA fibrillation and reduced biofilm formation in Salmonella typhimurium. Moreover, as previously shown, CsgA fibrils cross-seeded fibrillation of amyloid-β, providing support for the proposed structural resemblance and potential for cross-species amyloid interactions. The presented findings provide structural insights into amyloidogenic regions important for curli formation, suggest a novel strategy for disrupting amyloid-structured biofilms, and hypothesize on the formation of self-propagating prion-like species originating from a microbial source that could influence neurodegenerative diseases. PubMed: 31469892DOI: 10.1371/journal.ppat.1007978 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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