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X-ray structure of a functional full-length dynein motor domain

Nature Structural & Molecular Biology volume 18, pages 638642 (2011) | Download Citation

Abstract

Dyneins are large microtubule-based motors that power a wide variety of cellular processes. Here we report a 4.5-Å X-ray crystallographic analysis of the entire functional motor domain of cytoplasmic dynein with ADP from Dictyostelium discoideum, which has revealed the detailed architecture of the functional units required for motor activity, including the ATP-hydrolyzing ring, the long coiled-coil microtubule-binding stalk and the force-generating rod-like linker. We discovered a Y-shaped protrusion composed of two long coiled coils—the stalk and the newly identified 'strut'. This structure supports our model in which the strut coiled coil actively contributes to communication between the primary ATPase site in the ring and the microtubule-binding site at the tip of the stalk coiled coil. Our work also provides insight into how the two motor domains are arranged and how they interact with each other in a functional dimer form of cytoplasmic dynein.

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Protein Data Bank

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Acknowledgements

We thank E. Yamashita, Y. Umena, M. Suzuki and A. Nakagawa of the SPring-8 BL-44XU beamline, and Y. Yamada, N. Matsugaki, N. Igarashi and S. Wakatsuki of the Photon Factory, High Energy Accelerator Research Organization (KEK), for their support during X-ray data collection. We also thank R. Ohkura (University of Tokyo) and R. Shimo-Kon and T. Kikuchi (Osaka University) for their technical support. This work was supported by Grants-in-Aid for Scientific Research (17770126, 20687011 and 23370073 to T.K.; 16083205 and 17107003 to K.S.; 17053006, 18054008 and 20051006 to G.K.) from the Ministry of Education, Culture, Sports, Science and Technology of Japan, and by a grant from the Human Frontier Science Program (T.K.).

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Affiliations

  1. Institute for Protein Research, Osaka University, Osaka, Japan.

    • Takahide Kon
    •  & Genji Kurisu
  2. Department of Macromolecular Science, Graduate School of Science, Osaka University, Osaka, Japan.

    • Takahide Kon
    •  & Genji Kurisu
  3. Research Institute for Science and Engineering, Waseda University, Tokyo, Japan.

    • Kazuo Sutoh
  4. Precursory Research for Embryonic Science and Technology, Japan Science and Technology Agency, Saitama, Japan.

    • Genji Kurisu

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Contributions

T.K., K.S. and G.K. conceived of and designed the study. T.K. expressed, purified and crystallized the protein. T.K. and G.K. collected and analyzed the X-ray diffraction data. T.K., K.S. and G.K. wrote the paper.

Competing interests

The authors declare no competing financial interests.

Corresponding authors

Correspondence to Kazuo Sutoh or Genji Kurisu.

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https://doi.org/10.1038/nsmb.2074

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