Kreutzberger, Mark A. B.Sobe, Richard C.Sauder, Amber B.Chatterjee, SharanyaPena, AlejandroWang, FengbinGiron, Jorge A.Kiessling, VolkerCosta, Tiago RD D.Conticello, Vincent P.Frankel, GadKendall, Melissa M.Scharf, Birgit E.Egelman, Edward H.2024-01-222024-01-222022-03-172041-172310.1038/s41467-022-29069-y (PII)https://hdl.handle.net/10919/117445Flagellar filaments function as the propellers of the bacterial flagellum and their supercoiling is key to motility. The outer domains on the surface of the filament are non-critical for motility in many bacteria and their structures and functions are not conserved. Here, we show the atomic cryo-electron microscopy structures for flagellar filaments from enterohemorrhagic Escherichia coli O157:H7, enteropathogenic E. coli O127:H6, Achromobacter, and Sinorhizobium meliloti, where the outer domains dimerize or tetramerize to form either a sheath or a screw-like surface. These dimers are formed by 180° rotations of half of the outer domains. The outer domain sheath (ODS) plays a role in bacterial motility by stabilizing an intermediate waveform and prolonging the tumbling of E. coli cells. Bacteria with these ODS and screw-like flagellar filaments are commonly found in soil and human intestinal environments of relatively high viscosity suggesting a role for the dimerization in these environments.14 page(s)application/pdfenCreative Commons Attribution 4.0 InternationalFlagellaHumansBacteriaEscherichia coliFlagellinSoilCryoelectron MicroscopyDimerizationViscosityArticle - Refereedhttps://doi.org/10.1038/s41467-022-29069-y131Scharf, Birgit [0000-0001-6271-8972]353013062041-1723