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Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy

Author

Listed:
  • Koji Yonekura

    (Protonic NanoMachine Project, ERATO, JST
    Osaka University
    Dynamic NanoMachine Project, ICORP, JST)

  • Saori Maki-Yonekura

    (Protonic NanoMachine Project, ERATO, JST
    Dynamic NanoMachine Project, ICORP, JST)

  • Keiichi Namba

    (Protonic NanoMachine Project, ERATO, JST
    Osaka University
    Dynamic NanoMachine Project, ICORP, JST)

Abstract

The bacterial flagellar filament is a helical propeller for bacterial locomotion. It is a helical assembly of a single protein, flagellin, and its tubular structure is formed by 11 protofilaments in two distinct conformations, L- and R-type, for supercoiling. The X-ray crystal structure of a flagellin fragment lacking about 100 terminal residues revealed the protofilament structure, but the full filament structure is still essential for understanding the mechanism of supercoiling and polymerization. Here we report a complete atomic model of the R-type filament by electron cryomicroscopy. A density map obtained from image data up to 4 Å resolution shows the feature of α-helical backbone and some large side chains. The atomic model built on the map reveals intricate molecular packing and an α-helical coiled coil formed by the terminal chains in the inner core of the filament, with its intersubunit hydrophobic interactions having an important role in stabilizing the filament.

Suggested Citation

  • Koji Yonekura & Saori Maki-Yonekura & Keiichi Namba, 2003. "Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy," Nature, Nature, vol. 424(6949), pages 643-650, August.
  • Handle: RePEc:nat:nature:v:424:y:2003:i:6949:d:10.1038_nature01830
    DOI: 10.1038/nature01830
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    Cited by:

    1. William R Taylor & Teige R S Matthews-Palmer & Morgan Beeby, 2016. "Molecular Models for the Core Components of the Flagellar Type-III Secretion Complex," PLOS ONE, Public Library of Science, vol. 11(11), pages 1-33, November.
    2. Manuel Halte & Ekaterina P. Andrianova & Christian Goosmann & Fabienne F. V. Chevance & Kelly T. Hughes & Igor B. Zhulin & Marc Erhardt, 2024. "FlhE functions as a chaperone to prevent formation of periplasmic flagella in Gram-negative bacteria," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    3. Nicholas M Thomson & Josie L Ferreira & Teige R Matthews-Palmer & Morgan Beeby & Mark J Pallen, 2018. "Giant flagellins form thick flagellar filaments in two species of marine γ-proteobacteria," PLOS ONE, Public Library of Science, vol. 13(11), pages 1-12, November.
    4. Jessie Lynda Fields & Hua Zhang & Nathan F. Bellis & Holly A. Petersen & Sajal K. Halder & Shane T. Rich-New & Mart Krupovic & Hui Wu & Fengbin Wang, 2024. "Structural diversity and clustering of bacterial flagellar outer domains," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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