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Crystal structure of the motor domain of the kinesin-related motor ncd

Nature volume 380, pages 555–559 (1996)Cite this article

Abstract

MICROTUBULE-BASED ATPases of the kinesin superfamily1,2 provide the motile force for many animated features of living cells. Kinesin motors differ in their direction of movement along microtubules. Kinesin3 and ncd4,5, a kinesin-related motor involved in formation and maintenance of mitotic and meiotic spindles, move in opposite directions along microtubules, even though their motor domains are 40% identical in amino-acid sequence. Here we report the crystal structure of the MgADP complex of the Drosophila ncd motor domain determined to 2.5 Å by X-ray crystallography, and compare it to the kinesin structure. The ncd and kinesin motor domains are remarkably similar in structure, and the locations of conserved surface amino acids suggest these motors share a common microtubule-binding site. Moreover, structural and functional comparisons of ncd, kinesin, myosin and G proteins indicate that these NTPases may have a similar strategy of changing conformation between NTP and NDP states. We propose a general model for converting a common γ-phosphate-sensing mechanism into opposite polarities of movement for kinesin and ncd.

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Authors and Affiliations

  1. Department of Biochemistry/Biophysics, University of California, San Francisco, California, 94143, USA

    Elena P. Sablin, F. Jon Kull, Roger Cooke, Ronald D. Vale & Robert J. Fletterick

  2. Department of Pharmacology, University of California, San Francisco, California, 94143, USA

    Ronald D. Vale & Robert J. Fletterick

  3. The Howard Hughes Medical Institute, University of California, San Francisco, California, 94143, USA

    Ronald D. Vale

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  1. Elena P. Sablin
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  2. F. Jon Kull
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  3. Roger Cooke
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  4. Ronald D. Vale
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  5. Robert J. Fletterick
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Sablin, E., Jon Kull, F., Cooke, R. et al. Crystal structure of the motor domain of the kinesin-related motor ncd. Nature 380, 555–559 (1996). https://doi.org/10.1038/380555a0

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