ArticleCommunications biology2021
Structure of the bacterial flagellar hook cap provides insights into a hook assembly mechanism.
Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed.
- The structure of the complete extracellular bacterial flagellum reveals the mechanism of flagellin incorporation.Nature microbiology · 2025Article
- Genetic characteristics and potential pathogenic agents inEmerging microbes & infections · 2024Article
- Structure, Assembly, and Function of Flagella Responsible for Bacterial Locomotion.EcoSal Plus · 2023Review
- Virulence genotype and phenotype of two clinical isolates of Arcobacter butzleri obtained from patients with different pathologies.Archives of microbiology · 2023Article
- An overview of the structure and function of the flagellar hook FlgE protein.World journal of microbiology & biotechnology · 2023Review
- Loss of Flagella-Related Genes Enables a Nonflagellated, Fungal-Predating Bacterium To Strengthen the Synthesis of an Antifungal Weapon.Microbiology spectrum · 2023Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Assembly of bacterial flagellar hook requires FlgD, a protein known to form the hook cap. Symmetry mismatch between the hook and the hook cap is believed to drive efficient assembly of the hook in a way similar to the filament cap helping filament assembly. However, the hook cap dependent mechanism of hook assembly has remained poorly understood. Here, we report the crystal structure of the hook cap composed of five subunits of FlgD from Salmonella enterica at 3.3 Å resolution. The pentameric structure of the hook cap is divided into two parts: a stalk region composed of five N-terminal domains; and a petal region containing five C-terminal domains. Biochemical and genetic analyses show that the N-terminal domains of the hook cap is essential for the hook-capping function, and the structure now clearly reveals why. A plausible hook assembly mechanism promoted by the hook cap is proposed based on the structure.
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Registered trials
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