ArticleProceedings of the National Academy of Sciences of the United States of America2023
Tad and toxin-coregulated pilus structures reveal unexpected diversity in bacterial type IV pili.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 24 papers.
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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.
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Who cites it
24 citing papers in PubMed, 29 citations in OpenAlex.
- Structures of the Xcp and Hxc T2SS endopili provide new insights into type IV pili subfamilies.Structure (London, England : 1993) · 2026Article
- Insight into the relationship between type IV pilus function and biofilm formation.Biochemical Society transactions · 2026Review
- Article
- Visualization of Type IV Pili: Linking Structural Architecture, Dynamic Function, and Translational Opportunities.Biology · 2026Review
- Unveiling the genetic landscape and motility-associated functions of Type IV pili in theMicrobiome research reports · 2026Article
- Article
- Stimulation of themBio · 2025Article
- Electron Cryo-Tomography Reveals thebioRxiv : the preprint server for biology · 2025Article
- 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
- Article
- The structure of the Tad pilus alignment complex reveals a periplasmic conduit for pilus extension.Nature communications · 2025Article
- Tad pili with adaptable tips mediate contact-dependent killing during bacterial predation.Nature communications · 2025Article
- Structure and mechanism of human vesicular polyamine transporter.Nature communications · 2025Article
- Conformational changes in the motor ATPase CpaF facilitate a rotary mechanism of Tad pilus assembly.Nature communications · 2025Article
- Cryo-EM reconstruction of helical polymers: Beyond the simple cases.Quarterly reviews of biophysics · 2024Review
- Structure of the Pseudomonas aeruginosa PAO1 Type IV pilus.PLoS pathogens · 2024Article
- Structural diversity and clustering of bacterial flagellar outer domains.Nature communications · 2024Article
- Bidirectional pilus processing in the Tad pilus system motor CpaF.Nature communications · 2024Article
- Two distinct archaeal type IV pili structures formed by proteins with identical sequence.Nature communications · 2024Article
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Type IV pili (T4P) are ubiquitous in both bacteria and archaea. They are polymers of the major pilin protein, which has an extended and protruding N-terminal helix, α1, and a globular C-terminal domain. Cryo-EM structures have revealed key differences between the bacterial and archaeal T4P in their C-terminal domain structure and in the packing and continuity of α1. This segment forms a continuous α-helix in archaeal T4P but is partially melted in all published bacterial T4P structures due to a conserved helix breaking proline at position 22. The tad (tight adhesion) T4P are found in both bacteria and archaea and are thought to have been acquired by bacteria through horizontal transfer from archaea. Tad pilins are unique among the T4 pilins, being only 40 to 60 residues in length and entirely lacking a C-terminal domain. They also lack the Pro22 found in all high-resolution bacterial T4P structures. We show using cryo-EM that the bacterial tad pilus from
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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.