A structural change in the kinesin motor protein that drives motility

Sarah Rice, Abel W. Lin, Daniel Safer, Cynthia L. Hart, Nariman Naber, Bridget O. Carragher, Shane M. Cain, Elena Pechatnikova, Elizabeth M. Wilson-Kubalek, Michael Whittaker, Edward Pate, Roger Cooke, Edwin W. Taylor, Ronald A. Milligan and Ronald D. Vale ()
Additional contact information
Sarah Rice: Departments of Cellular and Molecular Pharmacology
Abel W. Lin: The Scripps Research Institute
Daniel Safer: University of Pennsylvania School of Medicine
Cynthia L. Hart: The Howard Hughes Medical Institute
Nariman Naber: Biochemistry and Biophysics, University of California
Bridget O. Carragher: Beckman Institute, University of Illinois at Urbana-Champaign
Shane M. Cain: The Scripps Research Institute
Elena Pechatnikova: University of Chicago
Elizabeth M. Wilson-Kubalek: The Scripps Research Institute
Michael Whittaker: The Scripps Research Institute
Edward Pate: Washington State University
Edwin W. Taylor: University of Chicago
Ronald A. Milligan: The Scripps Research Institute
Ronald D. Vale: The Howard Hughes Medical Institute

Nature, 1999, vol. 402, issue 6763, 778-784

Abstract: Abstract Kinesin motors power many motile processes by converting ATP energy into unidirectional motion along microtubules. The force-generating and enzymatic properties of conventional kinesin have been extensively studied; however, the structural basis of movement is unknown. Here we have detected and visualized a large conformational change of a ∼15-amino-acid region (the neck linker) in kinesin using electron paramagnetic resonance, fluorescence resonance energy transfer, pre-steady state kinetics and cryo-electron microscopy. This region becomes immobilized and extended towards the microtubule ‘plus’ end when kinesin binds microtubules and ATP, and reverts to a more mobile conformation when γ-phosphate is released after nucleotide hydrolysis. This conformational change explains both the direction of kinesin motion and processive movement by the kinesin dimer.

Date: 1999
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DOI: 10.1038/45483

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