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Comment
. 2007 Jan;189(2):291-3.
doi: 10.1128/JB.01556-06. Epub 2006 Nov 3.

How 34 pegs fit into 26 + 8 holes in the flagellar motor

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Comment

How 34 pegs fit into 26 + 8 holes in the flagellar motor

Michael D Manson. J Bacteriol. 2007 Jan.
No abstract available

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Figures

FIG. 1.
FIG. 1.
Schematic model for C-ring architecture in a CW-locked flagellar motor. (A) Two alternative associations of a FliM monomer with FliG. The middle domain of FliM is in cyan, the flexible GGXG-containing loop that contacts FliG is in red, the N-terminal sequence that binds phospho-CheY is in green, and the flexible connector between the CheY-binding sequence and the middle domain is indicated by the black line. FliG is shown as two blue-gray ovals (the inner N-terminal and outer C-terminal domains) joined by the helical connector (black line), with the EHPQ…R region in the N-terminal domain and the hydrophobic patch in the C-terminal domain both shown as black ovals. The MS ring is in yellow, the Mot protein complex is in magenta, the FliN tetramer is a blue ring, and the membrane is indicated by the elongated white rectangle. (B) Side view of a complete flagellar basal body. The color scheme is as in panel A but with the flagellar rod shown in black. (C) The FliG layer of the C ring looking toward the membrane from the cytoplasm. The motor is shown with 26 FliG subunits and 34 FliM subunits. The color scheme is as in panel A, with the hollow center of the MS ring shown in white. (D) The FliM layer of the C ring. Eight FliM subunits tilt inward to contact the EHPQ…R motif in the N-terminal domain of FliG. The remaining 26 FliM subunits orient with their long axes perpendicular to the C ring and contact the C-terminal motility domains of the FliG subunits. The orientation of the C ring in panels C and D is the same, so that the two images can be superimposed to reconstruct a C ring lacking only FliN. Note that the outward-facing FliM subunits flanking the inward-facing FliM subunits would have to splay out in order to contact the FliG motility domains at equal spacing, as shown in panel C. Alternatively, there could be gaps in the C ring at the level of the FliG motility domains, as suggested by Brown et al. (6).

Comment on

References

    1. Baker, M. D., P. M. Wolanin, and J. B. Stock. 2006. Signal transduction in bacterial chemotaxis. Bioessays 28:9-22. - PubMed
    1. Berry, R. M., and J. P. Armitage. 1999. The bacterial flagella motor. Adv. Microb. Physiol. 41:291-337. - PubMed
    1. Blair, D. F., and H. C. Berg. 1988. Restoration of torque in defective flagellar motors. Science 242:1678-1681. - PubMed
    1. Braun, T. F., L. Q. Al-Mawsawi, S. Kojima, and D. F. Blair. 2004. Arrangement of core membrane segments in the MotA/MotB proton-channel complex of Escherichia coli. Biochemistry 43:35-45. - PubMed
    1. Brown, P. N., C. P. Hill, and D. F. Blair. 2002. Crystal structure of the middle and C-terminal domains of the flagellar rotor protein FliG. EMBO J. 21:3225-3234. - PMC - PubMed

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