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Three-dimensional structure of a tubulin-motor-protein complex

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Abstract

THE kinesin superfamily is a class of microtubule-based mechano-enzymes involved in intracellular transport and chromosome movements. Molecules that move towards either the plus end or the minus end of micro tubules are represented within the family. The motor domains of these molecules exhibit considerable sequence homology and contain both the ATP- and microtubule-binding sites (reviewed in refs 1, 2). Here we focus on non-claret disjunctional (ncd), a minus-end-directed motor involved in chromosome segregation in meiosis and early mitosis in Drosophila3‡-6. We have calculated a three-dimensional map of tubulin sheets decorated with monomeric recombinant ncd motor domains7 by negative-stain electron microscopy and image analysis. Comparisons with a control structure of tubulin alone reveal that each motor domain binds to the crest of a single protofilament, making extensive contacts with both the α and β tubulin monomers. Binding of the motor domain results in significant conformational changes in both of the tubulin monomers.

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Authors and Affiliations

  1. Department of Cell Biology, The Scripps Research Institute, 10666 North Torrey Pines Road, La Jolla, California, 92037, USA

    Andreas Hoenger & Ronald A. Milligan

  2. Departments of Biochemistry and Biophysics, University of California, San Francisco, California, 94143, USA

    Elena P. Sablin & Robert J. Fletterick

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

    Ronald D. Vale

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

    Ronald D. Vale

Authors
  1. Andreas Hoenger
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  2. Elena P. Sablin
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  3. Ronald D. Vale
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  4. Robert J. Fletterick
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  5. Ronald A. Milligan
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Hoenger, A., Sablin, E., Vale, R. et al. Three-dimensional structure of a tubulin-motor-protein complex. Nature 376, 271–274 (1995). https://doi.org/10.1038/376271a0

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