ArticleStructure (London, England : 1993)2019
Structure and Assembly of the Enterohemorrhagic Escherichia coli Type 4 Pilus.
Article in Structure (London, England : 1993), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 50 citations in OpenAlex.
- Structural insights into the secretin complex of a type IVb pilus system.Nature communications · 2025Article
- Integrative Structure and Function of thebioRxiv : the preprint server for biology · 2025Article
- Type IV pili ofEcoSal Plus · 2024Review
- Structure of the Pseudomonas aeruginosa PAO1 Type IV pilus.PLoS pathogens · 2024Article
- Tight-packing of large pilin subunits provides distinct structural and mechanical properties for theProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Structure and Dynamics of Type 4a Pili and Type 2 Secretion System Endopili.Sub-cellular biochemistry · 2024Review
- Structure of a heteropolymeric type 4 pilus from a monoderm bacterium.Nature communications · 2023Article
- Microbial nanowires: type IV pili or cytochrome filaments?Trends in microbiology · 2023Review
- Mechanism of assembly of type 4 filaments: everything you always wanted to know (but were afraid to ask).Microbiology (Reading, England) · 2023Review
- Cryo-EM structure of an extracellular Geobacter OmcE cytochrome filament reveals tetrahaem packing.Nature microbiology · 2022Article
- The Type IV Pilus of Plasmid TP114 Displays Adhesins Conferring Conjugation Specificity and Is Important for DNA Transfer in the Mouse Gut Microbiota.Microbiology spectrum · 2022Article
- Host-Pathogen Adhesion as the Basis of Innovative Diagnostics for Emerging Pathogens.Diagnostics (Basel, Switzerland) · 2021Review
- Structure Determination of Microtubules and Pili: Past, Present, and Future Directions.Frontiers in molecular biosciences · 2021Review
- Architecture of the flexible tail tube of bacteriophage SPP1.Nature communications · 2020Article
- More than a feeling: microscopy approaches to understanding surface-sensing mechanisms.Journal of bacteriology · 2020Review
- CryoEM structure of the type IVa pilus secretin required for natural competence in Vibrio cholerae.Nature communications · 2020Article
- Structure and function of minor pilins of type IV pili.Medical microbiology and immunology · 2020Review
- Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium.Nature communications · 2020Article
- Repertoire of morphable proteins in an organism.PeerJ · 2020Article
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 2 countries.
Funding
Abstract
Bacterial type 4a pili are dynamic surface filaments that promote bacterial adherence, motility, and macromolecular transport. Their genes are highly conserved among enterobacteria and their expression in enterohemorrhagic Escherichia coli (EHEC) promotes adhesion to intestinal epithelia and pro-inflammatory signaling. To define the molecular basis of EHEC pilus assembly, we determined the structure of the periplasmic domain of its major subunit PpdD (PpdDp), a prototype of an enterobacterial pilin subfamily containing two disulfide bonds. The structure of PpdDp, determined by NMR, was then docked into the density envelope of purified EHEC pili obtained by cryoelectron microscopy (cryo-EM). Cryo-EM reconstruction of EHEC pili at ∼8 Å resolution revealed extremely high pilus flexibility correlating with a large extended region of the pilin stem. Systematic mutagenesis combined with functional and interaction analyses identified charged residues essential for pilus assembly. Structural information on exposed regions and interfaces between EHEC pilins is relevant for vaccine and drug discovery.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.