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A structural change in the kinesin motor protein that drives motility

Academic Article
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Overview

authors

  • Rice, S.
  • Lin, A. W.
  • Safer, D.
  • Hart, C. L.
  • Naber, N.
  • Carragher, Bridget
  • Cain, S. M.
  • Pechatnikova, E.
  • Wilson-Kubalek, Liz
  • Whittaker, M.
  • Pate, E.
  • Cooke, R.
  • Taylor, E. W.
  • Milligan, Ronald
  • Vale, R. D.

publication date

  • December 1999

journal

  • Nature  Journal

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 an approximately 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 gamma-phosphate is released after nucleotide hydrolysis. This conformational change explains both the direction of kinesin motion and processive movement by the kinesin dimer.

subject areas

  • Adenosine Triphosphatases
  • Cloning, Molecular
  • Cryoelectron Microscopy
  • Cysteine
  • Humans
  • Kinesin
  • Microtubules
  • Models, Molecular
  • Molecular Motor Proteins
  • Mutagenesis
  • Protein Conformation
  • Recombinant Proteins
  • Spectrometry, Fluorescence
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Identity

International Standard Serial Number (ISSN)

  • 0028-0836

Digital Object Identifier (DOI)

  • 10.1038/45483

PubMed ID

  • 10617199
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Additional Document Info

start page

  • 778

end page

  • 784

volume

  • 402

issue

  • 6763

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