Structural highlights
Function[FLAA_RHIML] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. Homomer of FlaA is able to form a functional filament. Publication Abstract from PubMedFlagellar 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 degrees 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. Flagellin outer domain dimerization modulates motility in pathogenic and soil bacteria from viscous environments.,Kreutzberger MAB, Sobe RC, Sauder AB, Chatterjee S, Pena A, Wang F, Giron JA, Kiessling V, Costa TRD, Conticello VP, Frankel G, Kendall MM, Scharf BE, Egelman EH Nat Commun. 2022 Mar 17;13(1):1422. doi: 10.1038/s41467-022-29069-y. PMID:35301306[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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