ArticleNature microbiology2025
The structure of the complete extracellular bacterial flagellum reveals the mechanism of flagellin incorporation.
Article in Nature microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed.
- The structure of the Vibrio alginolyticus flagellar filament suggests molecular mechanism for the rotation of sheathed flagella.Nature communications · 2026Article
- Assembly and glycosylation ofPNAS nexus · 2026Article
- A novel extracytoplasmic function sigma factor (RpoE6) regulates biogenesis of a minor flagellin and other functions inJournal of bacteriology · 2026Article
- Article
- The ancient E-ring in bacterial flagellar motors.FEMS microbiology reviews · 2026Review
- Ultraweak interactions drive cap-mediated positioning and elongation of the bacterial flagellar filament.Nature communications · 2025Article
- Curvature Generation and Engineering Principles fromACS nano · 2025Article
Corrections and comments
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Authors and funding
13 authors.
Funding
Abstract
The bacterial flagellum is essential for motility, adhesion and colonization in pathogens such as Salmonella enterica and Campylobacter jejuni. Its extracellular structure comprises the hook, hook-filament junction, filament and filament cap. Native structures of the hook-filament junction and the cap are lacking, and molecular mechanisms of cap-mediated filament assembly are largely uncharacterized. Here we use cryo-electron microscopy to resolve structures of the complete Salmonella extracellular flagellum including the pentameric FliD cap complex (3.7 Å) and the FlgKL hook-filament junction (2.9 Å), as well as the Campylobacter extracellular flagellum before filament assembly (6.5 Å). This, coupled with structure-guided mutagenesis and functional assays, reveals intermediates of filament assembly, showing that FliD cap protein terminal domain movement and clockwise rotation enable flagellin incorporation and stabilization of the filament. We show that the hook-filament junction acts as a buffer, preventing transfer of mechanical stress to the filament, and reveal the structural basis for the initiation of filament assembly. Collectively, this study provides comprehensive insights into flagellum assembly and how flagellin incorporation is coupled with its secretion.
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Registered trials
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