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; Ronald D. Vale

doi:10.1038/45483

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, Ronald D. Vale^*

^*Corresponding author for this work

Cell & Developmental Biology

Research output: Contribution to journal › Article › peer-review

661 Scopus citations

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.

Original language	English (US)
Pages (from-to)	778-784
Number of pages	7
Journal	Nature
Volume	402
Issue number	6763
DOIs	https://doi.org/10.1038/45483
State	Published - Dec 16 1999

ASJC Scopus subject areas

Medicine(all)
General

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title = "A structural change in the kinesin motor protein that drives motility",

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.",

author = "Sarah Rice and Lin, {Abel W.} and Daniel Safer and Hart, {Cynthia L.} and Nariman Naber and Carragher, {Bridget O.} and Cain, {Shane M.} and Elena Pechatnikova and Wilson-Kubalek, {Elizabeth M.} and Michael Whittaker and Edward Pate and Roger Cooke and Taylor, {Edwin W.} and Milligan, {Ronald A.} and Vale, {Ronald D.}",

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doi = "10.1038/45483",

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T1 - A structural change in the kinesin motor protein that drives motility

AU - Rice, Sarah

AU - Lin, Abel W.

AU - Safer, Daniel

AU - Hart, Cynthia L.

AU - Naber, Nariman

AU - Carragher, Bridget O.

AU - Cain, Shane M.

AU - Pechatnikova, Elena

AU - Wilson-Kubalek, Elizabeth M.

AU - Whittaker, Michael

AU - Pate, Edward

AU - Cooke, Roger

AU - Taylor, Edwin W.

AU - Milligan, Ronald A.

AU - Vale, Ronald D.

PY - 1999/12/16

Y1 - 1999/12/16

N2 - 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.

AB - 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.

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A structural change in the kinesin motor protein that drives motility

Abstract

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