ArticleProceedings of the National Academy of Sciences of the United States of America2016
Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 24 citations in OpenAlex.
- From Environmental Persistence to Host Adaptation: Differential Curli Regulation inMicroorganisms · 2026Review
- Structural insight intomBio · 2024Article
- Half a century of amyloids: past, present and future.Chemical Society reviews · 2020Review
- Cryo-EM structure of the nonameric CsgG-CsgF complex and its implications for controlling curli biogenesis in Enterobacteriaceae.PLoS biology · 2020Article
- NMR insights into the pre-amyloid ensemble and secretion targeting of the curli subunit CsgA.Scientific reports · 2020Article
- Assembly and substrate recognition of curli biogenesis system.Nature communications · 2020Article
- Bacterial functional amyloids: Order from disorder.Biochimica et biophysica acta. Proteins and proteomics · 2019Review
- Structural Insights into Curli CsgA Cross-β Fibril Architecture Inspire Repurposing of Anti-amyloid Compounds as Anti-biofilm Agents.PLoS pathogens · 2019Article
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- Periplasmic Chaperones and Prolyl Isomerases.EcoSal Plus · 2018Review
- The Production of Curli Amyloid Fibers Is Deeply Integrated into the Biology of Escherichia coli.Biomolecules · 2017Article
- A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis.Nature communications · 2017Article
- Nucleation and growth of a bacterial functional amyloid at single-fiber resolution.Nature chemical biology · 2017Article
- Structural insights into functional amyloid inhibition in Gram -ve bacteria.Biochemical Society transactions · 2016Review
- Purification, crystallization and characterization of the Pseudomonas outer membrane protein FapF, a functional amyloid transporter.Acta crystallographica. Section F, Structural biology communications · 2016Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Curli, consisting primarily of major structural subunit CsgA, are functional amyloids produced on the surface of Escherichia coli, as well as many other enteric bacteria, and are involved in cell colonization and biofilm formation. CsgE is a periplasmic accessory protein that plays a crucial role in curli biogenesis. CsgE binds to both CsgA and the nonameric pore protein CsgG. The CsgG-CsgE complex is the curli secretion channel and is essential for the formation of the curli fibril in vivo. To better understand the role of CsgE in curli formation, we have determined the solution NMR structure of a double mutant of CsgE (W48A/F79A) that appears to be similar to the wild-type (WT) protein in overall structure and function but does not form mixed oligomers at NMR concentrations similar to the WT. The well-converged structure of this mutant has a core scaffold composed of a layer of two α-helices and a layer of three-stranded antiparallel β-sheet with flexible N and C termini. The structure of CsgE fits well into the cryoelectron microscopy density map of the CsgG-CsgE complex. We highlight a striking feature of the electrostatic potential surface in CsgE structure and present an assembly model of the CsgG-CsgE complex. We suggest a structural mechanism of the interaction between CsgE and CsgA. Understanding curli formation can provide the information necessary to develop treatments and therapeutic agents for biofilm-related infections and may benefit the prevention and treatment of amyloid diseases. CsgE could establish a paradigm for the regulation of amyloidogenesis because of its unique role in curli formation.
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