ArticleScientific reports2017
Structure of FlgK reveals the divergence of the bacterial Hook-Filament Junction of Campylobacter.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- Ultraweak interactions drive cap-mediated positioning and elongation of the bacterial flagellar filament.Nature communications · 2025Article
- Divergent immune responses to commensal bacteria bearing distinct motility signatures.Science immunology · 2025Article
- Rescue of bacterial motility using two- and three-species FliC chimeras.Journal of bacteriology · 2025Article
- Curvature Generation and Engineering Principles fromACS nano · 2025Article
- The structure of the complete extracellular bacterial flagellum reveals the mechanism of flagellin incorporation.Nature microbiology · 2025Article
- Structure and Dynamics of the Bacterial Flagellar Motor Complex.Biomolecules · 2024Review
- Helicobacter pylori FlgN binds its substrate FlgK and the flagellum ATPase FliI in a similar manner observed for the FliT chaperone.Protein science : a publication of the Protein Society · 2024Article
- Structure, Assembly, and Function of Flagella Responsible for Bacterial Locomotion.EcoSal Plus · 2023Review
- Campylobacter jejuni: targeting host cells, adhesion, invasion, and survival.Applied microbiology and biotechnology · 2023Review
- The Missing Pieces: The Role of Secretion Systems inBiomolecules · 2023Review
- Large-scale discovery of protein interactions at residue resolution using co-evolution calculated from genomic sequences.Nature communications · 2021Article
- Structural Conservation and Adaptation of the Bacterial Flagella Motor.Biomolecules · 2020Review
- Crystal structure of FlgL and its implications for flagellar assembly.Scientific reports · 2018Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Evolution of a nano-machine consisting of multiple parts, each with a specific function, is a complex process. A change in one part should eventually result in changes in other parts, if the overall function is to be conserved. In bacterial flagella, the filament and the hook have distinct functions and their respective proteins, FliC and FlgE, have different three-dimensional structures. The filament functions as a helical propeller and the hook as a flexible universal joint. Two proteins, FlgK and FlgL, assure a smooth connectivity between the hook and the filament. Here we show that, in Campylobacter, the 3D structure of FlgK differs from that of its orthologs in Salmonella and Burkholderia, whose structures have previously been solved. Docking the model of the FlgK junction onto the structure of the Campylobacter hook provides some clues about its divergence. These data suggest how evolutionary pressure to adapt to structural constraints, due to the structure of Campylobacter hook, causes divergence of one element of a supra-molecular complex in order to maintain the function of the entire flagellar assembly.
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