ArticleNature communications2024
Two distinct archaeal type IV pili structures formed by proteins with identical sequence.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Structures of the Xcp and Hxc T2SS endopili provide new insights into type IV pili subfamilies.Structure (London, England : 1993) · 2026Article
- Sulfolobales: Acidothermophilic archaea as models for biology and biotechnological applications.Engineering microbiology · 2026Review
- Successive waves of transcriptional repression and de-repression license cell cycle progression in an archaeon.Nucleic acids research · 2026Article
- PilY proteins: bimodular drivers of type IV pilus versatility.Trends in microbiology · 2026Review
- Structural insights into the secretin complex of a type IVb pilus system.Nature communications · 2025Article
- A family of tubular pili from harmful algal bloom forming cyanobacterium Microcystis aeruginosa.Nature communications · 2025Article
- Cryo-EM for atomic characterization of supramolecular gels.Faraday discussions · 2025Article
- Tat-dependent bundling pilus of a halophilic archaeon assembles by a strand donation mechanism and facilitates biofilm formation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A type IV pili-mediated mutualism between two co-resident temperate archaeal viruses and their host.Cell reports · 2025Article
- Transcriptional landscape of the cell cycle in a model thermoacidophilic archaeon reveals similarities to eukaryotes.Nature communications · 2025Article
- Fragment-Based Approach for Hierarchical Nanotube Assembly of Small Molecules in Aqueous Phase.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Unusual cell surfaces, pili, and archaella of Thermoplasmatales archaea.The ISME journal · 2025Article
- Cryo-EM reconstruction of helical polymers: Beyond the simple cases.Quarterly reviews of biophysics · 2024Review
- Towards a molecular picture of the archaeal cell surface.Nature communications · 2024Article
- Structural diversity and clustering of bacterial flagellar outer domains.Nature communications · 2024Article
- Cell-Free Nonequilibrium Assembly for Hierarchical Protein/Peptide Nanopillars.Journal of the American Chemical Society · 2024Article
- Perturbed N-glycosylation of Halobacterium salinarum archaellum filaments leads to filament bundling and compromised cell motility.Nature communications · 2024Article
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Abstract
Type IV pili (T4P) represent one of the most common varieties of surface appendages in archaea. These filaments, assembled from small pilin proteins, can be many microns long and serve diverse functions, including adhesion, biofilm formation, motility, and intercellular communication. Here, we determine atomic structures of two distinct adhesive T4P from Saccharolobus islandicus via cryo-electron microscopy (cryo-EM). Unexpectedly, both pili were assembled from the same pilin polypeptide but under different growth conditions. One filament, denoted mono-pilus, conforms to canonical archaeal T4P structures where all subunits are equivalent, whereas in the other filament, the tri-pilus, the same polypeptide exists in three different conformations. The three conformations in the tri-pilus are very different from the single conformation found in the mono-pilus, and involve different orientations of the outer immunoglobulin-like domains, mediated by a very flexible linker. Remarkably, the outer domains rotate nearly 180° between the mono- and tri-pilus conformations. Both forms of pili require the same ATPase and TadC-like membrane pore for assembly, indicating that the same secretion system can produce structurally very different filaments. Our results show that the structures of archaeal T4P appear to be less constrained and rigid than those of the homologous archaeal flagellar filaments that serve as helical propellers.
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