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The 2.8 Å crystal structure of the dynein motor domain

Author

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  • Takahide Kon

    (Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan
    Graduate School of Science, Osaka University)

  • Takuji Oyama

    (Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan)

  • Rieko Shimo-Kon

    (Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan)

  • Kenji Imamula

    (Graduate School of Arts and Sciences, University of Tokyo)

  • Tomohiro Shima

    (Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyou-ku, Tokyo 113-0033, Japan)

  • Kazuo Sutoh

    (Research Institute for Science and Engineering, Waseda University, Takada 1-17-22, Toshima-ku, Tokyo 171-0033, Japan)

  • Genji Kurisu

    (Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan
    Graduate School of Science, Osaka University)

Abstract

Dyneins are microtubule-based AAA+ motor complexes that power ciliary beating, cell division, cell migration and intracellular transport. Here we report the most complete structure obtained so far, to our knowledge, of the 380-kDa motor domain of Dictyostelium discoideum cytoplasmic dynein at 2.8 Å resolution; the data are reliable enough to discuss the structure and mechanism at the level of individual amino acid residues. Features that can be clearly visualized at this resolution include the coordination of ADP in each of four distinct nucleotide-binding sites in the ring-shaped AAA+ ATPase unit, a newly identified interaction interface between the ring and mechanical linker, and junctional structures between the ring and microtubule-binding stalk, all of which should be critical for the mechanism of dynein motility. We also identify a long-range allosteric communication pathway between the primary ATPase and the microtubule-binding sites. Our work provides a framework for understanding the mechanism of dynein-based motility.

Suggested Citation

  • Takahide Kon & Takuji Oyama & Rieko Shimo-Kon & Kenji Imamula & Tomohiro Shima & Kazuo Sutoh & Genji Kurisu, 2012. "The 2.8 Å crystal structure of the dynein motor domain," Nature, Nature, vol. 484(7394), pages 345-350, April.
    • Handle: RePEc:nat:nature:v:484:y:2012:i:7394:d:10.1038_nature10955
    DOI: 10.1038/nature10955
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