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6G9G

Crystal Structure of the TASNSS segment from the R4-R5 loop of the E. coli Biofilm-associated CsgA Curli protein

Summary for 6G9G
Entry DOI10.2210/pdb6g9g/pdb
DescriptorMajor curlin subunit (2 entities in total)
Functional Keywordsbacterial fibril from e. coli, protein fibril
Biological sourceEscherichia coli
Total number of polymer chains1
Total formula weight565.53
Authors
Landau, M.,Perov, S. (deposition date: 2018-04-10, release date: 2019-04-24, Last modification date: 2024-05-08)
Primary citationPerov, 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: 31469892
DOI: 10.1371/journal.ppat.1007978
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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