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Conformational change of flagellin for polymorphic supercoiling of the flagellar filament

Nature Structural & Molecular Biology volume 17, pages 417–422 (2010)Cite this article

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Abstract

The bacterial flagellar filament is a helical propeller rotated by the flagellar motor for bacterial locomotion. The filament is a supercoiled assembly of a single protein, flagellin, and is formed by 11 protofilaments. For bacterial taxis, the reversal of motor rotation switches the supercoil between left- and right-handed, both of which arise from combinations of two distinct conformations and packing interactions of the L-type and R-type protofilaments. Here we report an atomic model of the L-type straight filament by electron cryomicroscopy and helical image analysis. Comparison with the R-type structure shows interesting features: an orientation change of the outer core domains (D1) against the inner core domains (D0) showing almost invariant orientation and packing, a conformational switching within domain D1, and the conformational flexibility of domains D0 and D1 with their spoke-like connection for tight molecular packing.

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Figure 1: Ribbon diagram of the Cα backbone of the filament models.
Figure 2: Comparison of the Cα backbones of L-type (blue) and R-type (red) flagellin in stereo.
Figure 3: Superposition of the L-type (blue) and R-type (red) filament structures showing the overall switching in the orientation of domains D1, D2 and D3 against the inner tube structure made of D0 domains, viewed in stereo.
Figure 4: Conformational changes that may be responsible for the switching.

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Acknowledgements

We thank C. Toyoshima for part of the helical image reconstruction programs, D.A. Agard and J.W. Sedat for support to S.M.-Y. and K.Y. and F. Oosawa, S. Asakura and D.L.D. Caspar for continuous support and encouragement. This work was partly supported by funds from the W.M. Keck Advanced Microscopy Laboratory at the University of California, San Francisco, to K.Y. and by Grants-in-Aid for Scientific Research (16087207) 'National Project on Protein Structural and Functional Analyses' from the Ministry of Education, Science and Culture of Japan to K.N.

Author information

Authors and Affiliations

  1. Dynamic NanoMachine Project, International Cooperative Research Project, Japan Science and Technology Agency, Suita, Osaka, Japan.,

    Saori Maki-Yonekura & Keiichi Namba

  2. Department of Biochemistry and Biophysics, The W.M. Keck Advanced Microscopy Laboratory, University of California, San Francisco, San Francisco, California, USA.,

    Saori Maki-Yonekura & Koji Yonekura

  3. Protein Crystallography Research Group, RIKEN SPring-8 Center, Harima Institute, Sayo, Hyogo, Japan.,

    Saori Maki-Yonekura

  4. Biostructural Mechanism Laboratory, RIKEN SPring-8 Center, Harima Institute, Sayo, Hyogo, Japan.,

    Koji Yonekura

  5. Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan.,

    Keiichi Namba

Authors
  1. Saori Maki-Yonekura
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Contributions

S.M.-Y. prepared filament samples, collected electron cryomicroscopy images, analyzed images and carried out model building; K.Y. developed programs for graphical user interface, spline fitting and superimposition of the molecular models of the L- and R-type filaments; K.Y. also supervised all the computational analysis; S.M.-Y., K.Y. and K.N. wrote the paper.

Corresponding authors

Correspondence to Koji Yonekura or Keiichi Namba.

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The authors declare no competing financial interests.

Supplementary information

Supplementary Text and Figures

Supplementary Figures 1 and 2, Supplementary Tables 1–3 (PDF 1614 kb)

Supplementary Movie 1

Transition between the L-type and R-type straight filaments in stereo (MOV 763 kb)

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Maki-Yonekura, S., Yonekura, K. & Namba, K. Conformational change of flagellin for polymorphic supercoiling of the flagellar filament. Nat Struct Mol Biol 17, 417–422 (2010). https://doi.org/10.1038/nsmb.1774

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