Divergence of Quaternary Structures Among Bacterial Flagellar Filaments

  title={Divergence of Quaternary Structures Among Bacterial Flagellar Filaments},
  author={Vitold E. Galkin and Xiong Yu and Jakub A. Bielnicki and John E. Heuser and Cheryl Ewing and Patricia Guerry and Edward H. Egelman},
  pages={382 - 385}
It has been widely assumed that the atomic structure of the flagellar filament from Salmonella typhimurium serves as a model for all bacterial flagellar filaments given the sequence conservation in the coiled-coil regions responsible for polymerization. On the basis of electron microscopic images, we show that the flagellar filaments from Campylobacter jejuni have seven protofilaments rather than the 11 in S. typhimurium. The vertebrate Toll-like receptor 5 (TLR5) recognizes a region of… 
Complete structure of the bacterial flagellar hook reveals extensive set of stabilizing interactions
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Atomic structure of the Campylobacter jejuni flagellar filament reveals how ε Proteobacteria escaped Toll-like receptor 5 surveillance
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A structural model of flagellar filament switching across multiple bacterial species
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Archaeal flagellin combines a bacterial type IV pilin domain with an Ig-like domain
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Structural insights into bacterial flagellar hooks similarities and specificities
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Bacterial flagellar capping proteins adopt diverse oligomeric states
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Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy
A complete atomic model of the R-type filament by electron cryomicroscopy reveals intricate molecular packing and an α-helical coiled coil formed by the terminal chains in the inner core of the filament, with its intersubunit hydrophobic interactions having an important role in stabilizing the filament.
Structure and switching of bacterial flagellar filaments studied by X-ray fiber diffraction
Based on the measured helical parameters of the L and R lattices and the switching model, the twist and curvature calculated for the ten possible supercoils are in quantitative accord with observed supercoiled forms of flagellar filaments.
Evasion of Toll-like receptor 5 by flagellated bacteria.
The results suggest that TLR5 evasion is critical for the survival of this subset of bacteria at mucosal sites in animals and raise the intriguing possibility that flagellin receptors provided the selective force to drive the evolution of these unique subclasses of bacterial flageLLins.
Toll-like receptor 5 recognizes a conserved site on flagellin required for protofilament formation and bacterial motility
The exquisite ability of the innate immune system to precisely target a conserved site on flagellin that is essential for bacterial motility is demonstrated.
The structure of bacterial ParM filaments
Using cryo-EM and three-dimensional reconstruction, it is shown that ParM filaments have a different structure from F-actin, with very different subunit-subunit interfaces, and that this involves domain-domain rotations within the ParM subunit.
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Although the wild-type flagellar filament is a heteropolymer of the flaA andflaB gene products, immunogold electron microscopy suggests that flaB epitopes are poorly surface exposed along the length of theWild-type filament.
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