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@ARTICLE{Braun:820059,
      author       = {Braun, Tatjana and Vos, Matthijn R. and Kalisman, Nir and
                      Sherman, Nicholas E. and Rachel, Reinhard and Wirth,
                      Reinhard and Schröder, Gunnar and Egelman, Edward H.},
      title        = {{A}rchaeal flagellin combines a bacterial type {IV} pilin
                      domain with an {I}g-like domain},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {113},
      number       = {37},
      issn         = {1091-6490},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {FZJ-2016-05616},
      pages        = {10352 - 10357},
      year         = {2016},
      abstract     = {The bacterial flagellar apparatus, which involves ∼40
                      different proteins, has been a model system for
                      understanding motility and chemotaxis. The bacterial
                      flagellar filament, largely composed of a single protein,
                      flagellin, has been a model for understanding protein
                      assembly. This system has no homology to the eukaryotic
                      flagellum, in which the filament alone, composed of a
                      microtubule-based axoneme, contains more than 400 different
                      proteins. The archaeal flagellar system is simpler still, in
                      some cases having ∼13 different proteins with a single
                      flagellar filament protein. The archaeal flagellar system
                      has no homology to the bacterial one and must have arisen by
                      convergent evolution. However, it has been understood that
                      the N-terminal domain of the archaeal flagellin is a homolog
                      of the N-terminal domain of bacterial type IV pilin, showing
                      once again how proteins can be repurposed in evolution for
                      different functions. Using cryo-EM, we have been able to
                      generate a nearly complete atomic model for a flagellar-like
                      filament of the archaeon Ignicoccus hospitalis from a
                      reconstruction at ∼4-Å resolution. We can now show that
                      the archaeal flagellar filament contains a β-sandwich,
                      previously seen in the FlaF protein that forms the anchor
                      for the archaeal flagellar filament. In contrast to the
                      bacterial flagellar filament, where the outer globular
                      domains make no contact with each other and are not
                      necessary for either assembly or motility, the archaeal
                      flagellin outer domains make extensive contacts with each
                      other that largely determine the interesting mechanical
                      properties of these filaments, allowing these filaments to
                      flex.},
      cin          = {ICS-6},
      ddc          = {000},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000383092000046},
      pubmed       = {pmid:27578865},
      doi          = {10.1073/pnas.1607756113},
      url          = {https://juser.fz-juelich.de/record/820059},
}