<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Einenkel R</submitter><funding>European Research Council</funding><funding>Human Frontier Science Program (HFSP)</funding><funding>Biotechnology and Biological Sciences Research Council</funding><pagination>1741-1757</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12221982</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>10(7)</volume><pubmed_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 filamen</pubmed_abstract><journal>Nature microbiology</journal><pubmed_title>The structure of the complete extracellular bacterial flagellum reveals the mechanism of flagellin incorporation.</pubmed_title><pmcid>PMC12221982</pmcid><funding_grant_id>BB/R009759/2</funding_grant_id><funding_grant_id>864971</funding_grant_id><funding_grant_id>RGY0080/2021</funding_grant_id><funding_grant_id>BB/V019732/1</funding_grant_id><pubmed_authors>Gonzalez-Rodriguez N</pubmed_authors><pubmed_authors>Harrowell J</pubmed_authors><pubmed_authors>Qin K</pubmed_authors><pubmed_authors>Al-Otaibi NS</pubmed_authors><pubmed_authors>Einenkel R</pubmed_authors><pubmed_authors>Schmidt J</pubmed_authors><pubmed_authors>Erhardt M</pubmed_authors><pubmed_authors>Beeby M</pubmed_authors><pubmed_authors>Mann D</pubmed_authors><pubmed_authors>Bergeron JRC</pubmed_authors><pubmed_authors>Drobnic T</pubmed_authors><pubmed_authors>Cohen EJ</pubmed_authors><pubmed_authors>Shmakova E</pubmed_authors></additional><is_claimable>false</is_claimable><name>The structure of the complete extracellular bacterial flagellum reveals the mechanism of flagellin incorporation.</name><description>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 filamen</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 Jul</publication><modification>2026-06-01T15:32:13.875Z</modification><creation>2026-04-08T13:46:46.609Z</creation></dates><accession>S-EPMC12221982</accession><cross_references><pubmed>40595287</pubmed><doi>10.1038/s41564-025-02037-0</doi></cross_references></HashMap>