ArticleStructure (London, England : 1993)2017
The Cryoelectron Microscopy Structure of the Type 1 Chaperone-Usher Pilus Rod.
Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- Water, water, every where-the advent of hydrated pili structure.The FEBS journal · 2026Article
- Antiparallel stacking of Csu pili drives Acinetobacter baumannii 3D biofilm assembly.Nature communications · 2026Article
- Donor strand complementation and calcium ion coordination drive the chaperone-free polymerization of archaeal cannulae.Nature communications · 2025Article
- Structures of the Escherichia coli type 1 pilus during pilus rod assembly and after assembly termination.Nature communications · 2025Article
- Tat-fimbriae ("tafi"): An unusual type of haloarchaeal surface structure depending on the twin-arginine translocation pathway.iScience · 2025Article
- The assembly platform FimD is required to obtain the most stable quaternary structure of type 1 pili.Nature communications · 2024Article
- The role of filamentous matrix molecules in shaping the architecture and emergent properties of bacterial biofilms.The Biochemical journal · 2024Review
- Stochastic chain termination in bacterial pilus assembly.Nature communications · 2023Article
- The polymer and materials science of the bacterial fimbriae Caf1.Biomaterials science · 2023Review
- Three structural solutions for bacterial adhesion pilus stability and superelasticity.Structure (London, England : 1993) · 2023Article
- TapA acts as specific chaperone in TasA filament formation by strand complementation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Electron cryo-microscopy reveals the structure of the archaeal thread filament.Nature communications · 2022Article
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- Archaeal bundling pili ofProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Unveiling molecular interactions that stabilize bacterial adhesion pili.Biophysical journal · 2022Article
- Protein nanowires with tunable functionality and programmable self-assembly using sequence-controlled synthesis.Nature communications · 2022Article
- Processive dynamics of the usher assembly platform during uropathogenic Escherichia coli P pilus biogenesis.Nature communications · 2021Article
- Impact of an alpha helix and a cysteine-cysteine disulfide bond on the resistance of bacterial adhesion pili to stress.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
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Abstract
Adhesive chaperone-usher pili are long, supramolecular protein fibers displayed on the surface of many bacterial pathogens. The type 1 and P pili of uropathogenic Escherichia coli (UPEC) play important roles during urinary tract colonization, mediating attachment to the bladder and kidney, respectively. The biomechanical properties of the helical pilus rods allow them to reversibly uncoil in response to flow-induced forces, allowing UPEC to retain a foothold in the unique and hostile environment of the urinary tract. Here we provide the 4.2-Å resolution cryo-EM structure of the type 1 pilus rod, which together with the previous P pilus rod structure rationalizes the remarkable "spring-like" properties of chaperone-usher pili. The cryo-EM structure of the type 1 pilus rod differs in its helical parameters from the structure determined previously by a hybrid approach. We provide evidence that these structural differences originate from different quaternary structures of pili assembled in vivo and in vitro.
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