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@ARTICLE{Einenkel:1050713,
      author       = {Einenkel, Rosa and Qin, Kailin and Schmidt, Julia and
                      Al-Otaibi, Natalie S. and Mann, Daniel and Drobnič, Tina
                      and Cohen, Eli J. and Gonzalez-Rodriguez, Nayim and
                      Harrowell, Jane and Shmakova, Elena and Beeby, Morgan and
                      Erhardt, Marc and Bergeron, Julien R. C.},
      title        = {{T}he structure of the complete extracellular bacterial
                      flagellum reveals the mechanism of flagellin incorporation},
      journal      = {Nature microbiology},
      volume       = {10},
      number       = {7},
      issn         = {2058-5276},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2026-00458},
      pages        = {1741-1757},
      year         = {2025},
      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.},
      cin          = {ER-C-3},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ER-C-3-20170113},
      pnm          = {5352 - Understanding the Functionality of Soft Matter and
                      Biomolecular Systems (POF4-535) / 5241 - Molecular
                      Information Processing in Cellular Systems (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5352 / G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1038/s41564-025-02037-0},
      url          = {https://juser.fz-juelich.de/record/1050713},
}