EMD-25213
Cryo-EM structure of the enteropathogenic E. coli O127:H6 flagellar filament
EMD-25213
Single-particle4.2 Å
Deposition: 27/10/2021Map released: 16/03/2022
Last modified: 05/06/2024
Sample Organism:
Escherichia coli O127:H6
Sample: Bacterial flagellar filament
Fitted models: 7sn7 (Avg. Q-score: 0.343)
Deposition Authors: Kreutzberger MAB, Chatterjee S
Sample: Bacterial flagellar filament
Fitted models: 7sn7 (Avg. Q-score: 0.343)
Deposition Authors: Kreutzberger MAB, Chatterjee S
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
(2022) Nat Commun , 13 , 1422 - 1422
,
Sauder AB,
Chatterjee S,
Pena A ,
Wang F ,
Giron JA,
Kiessling V ,
Costa TRD ,
Conticello VP ,
Frankel G ,
Kendall MM,
Scharf BE,
Egelman EH
(2022) Nat Commun , 13 , 1422 - 1422
Abstract:
Flagellar 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.
Flagellar 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.