6G8C

Crystal Structure of the Amyloid-like IYQYGG segment from the R1 repeat of the E. coli Biofilm-associated CsgA Curli protein

6G8C の概要

• エントリーDOI: 10.2210/pdb6g8c/pdb
• 分子名称: Major curlin subunit (2 entities in total)
• 機能のキーワード: bacterial steric-zipper cross-beta amyloid fibril from e. coli, protein fibril
• 由来する生物種: Escherichia coli K-12
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 699.75

構造登録者

Landau, M.,Perov, S. (登録日: 2018-04-08, 公開日: 2019-04-24, 最終更新日: 2024-05-01)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (1.65 Å)