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TitleThe three-dimensional structure of the flagellar rotor from a clockwise-locked mutant of Salmonella enterica serovar Typhimurium.
Journal, issue, pagesJ Bacteriol, Vol. 188, Issue 20, Page 7039-7048, Year 2006
Publish dateNov 6, 2006
AuthorsDennis R Thomas / Noreen R Francis / Chen Xu / David J DeRosier /
PubMed AbstractThree-dimensional reconstructions from electron cryomicrographs of the rotor of the flagellar motor reveal that the symmetry of individual M rings varies from 24-fold to 26-fold while that of the C ...Three-dimensional reconstructions from electron cryomicrographs of the rotor of the flagellar motor reveal that the symmetry of individual M rings varies from 24-fold to 26-fold while that of the C rings, containing the two motor/switch proteins FliM and FliN, varies from 32-fold to 36-fold, with no apparent correlation between the symmetries of the two rings. Results from other studies provided evidence that, in addition to the transmembrane protein FliF, at least some part of the third motor/switch protein, FliG, contributes to a thickening on the face of the M ring, but there was no evidence as to whether or not any portion of FliG also contributes to the C ring. Of the four morphological features in the cross section of the C ring, the feature closest to the M ring is not present with the rotational symmetry of the rest of the C ring, but instead it has the symmetry of the M ring. We suggest that this inner feature arises from a domain of FliG. We present a hypothetical docking in which the C-terminal motor domain of FliG lies in the C ring, where it can interact intimately with FliM.
External linksJ Bacteriol / PubMed:17015643 / PubMed Central
MethodsEM (single particle)
Structure data

EMDB-1887:
Flagellar basal body - Salmonella Typhimurium.
Method: EM (single particle)

Source
  • Salmonella enterica subsp. enterica serovar Typhimurium (bacteria)

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