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TitleStructures of the sheathed flagellum reveal mechanisms of assembly and rotation in Vibrio cholerae.
Journal, issue, pagesNat Microbiol, Vol. 10, Issue 12, Page 3305-3314, Year 2025
Publish dateOct 31, 2025
AuthorsWangbiao Guo / Sarah Zhang / Jin Hwan Park / Venus Stanton / Merrill Asp / Helen Herrera / Jung-Shen Benny Tai / Jian Yue / Jiaqi Wang / Jiaqi Guo / Rajeev Kumar / Jack M Botting / Shenping Wu / Jing Yan / Karl E Klose / Fitnat H Yildiz / Jun Liu /
PubMed AbstractMotility promotes the complex life cycle and infectious capabilities of Vibrio cholerae and is driven by rotation of a single polar flagellum. The flagellar filament comprises four flagellin proteins ...Motility promotes the complex life cycle and infectious capabilities of Vibrio cholerae and is driven by rotation of a single polar flagellum. The flagellar filament comprises four flagellin proteins (FlaA-D) and is covered by a membranous sheath continuous with the outer membrane. Here we combine in situ cryo-electron microscopy single-particle analysis, fluorescence microscopy and molecular genetics to determine 2.92-3.43 Å structures of the sheathed flagellar filament from intact bacteria. Our data reveal the spatial arrangement of FlaA-D, showing that FlaA localizes at the cell pole and functions as a template for filament assembly involving multiple flagellins. Unlike unsheathed flagellar filaments, the sheathed filament from V. cholerae possesses a highly conserved core but a smooth, hydrophilic surface adjacent to the membranous sheath. A tiny conformational change at the single flagellin level results in a supercoiled filament and curved membranous sheath, supporting a model wherein the filament rotates separately from the sheath, enabling the distinct motility of V. cholerae.
External linksNat Microbiol / PubMed:41174224
MethodsEM (single particle) / EM (helical sym.)
Resolution2.45 - 3.43 Å
Structure data

49125

9n8a

EMDB-49125, PDB-9n8a:
In situ structure of the sheathed FlaD flagellar filament in Vibrio cholerae
Method: EM (single particle) / Resolution: 2.92 Å

49126

9n8b

EMDB-49126, PDB-9n8b:
In situ unsheathed flagellar filament of Vibrio cholerae resolved with helical reconstruction.
Method: EM (helical sym.) / Resolution: 2.45 Å

49128

9n8g

EMDB-49128, PDB-9n8g:
In situ sheathed FlaA flagellar filament of Vibrio cholerae
Method: EM (single particle) / Resolution: 3.43 Å

49129

9n8h

EMDB-49129, PDB-9n8h:
In situ sheathed flagellar filament of Vibrio cholerae resolved with helical reconstruction.
Method: EM (helical sym.) / Resolution: 2.73 Å

49131

9n8m

EMDB-49131, PDB-9n8m:
In situ sheathed flagellar FlaC filament in Vibrio cholerae.
Method: EM (single particle) / Resolution: 3.16 Å

71351

9p7r

EMDB-71351, PDB-9p7r:
In situ structure of the sheathed FlaB flagellar filament in Vibrio cholerae
Method: EM (single particle) / Resolution: 3.16 Å

Source
  • vibrio cholerae o1 biovar el tor str. n16961 (bacteria)
  • vibrio cholerae o1 biovar el tor (bacteria)
KeywordsMOTOR PROTEIN / In situ cryo-EM / sheathed flagellar filament / FlaD Vibrio cholerae. / unsheathed flagellar filament / FlaC / Vibrio cholerae. / FlaB Vibrio cholerae.

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