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Nature. 1999 Dec 16;402(6763):778-84.

A structural change in the kinesin motor protein that drives motility.

Author information

1
Department of Cellular and Molecular Pharmacology, University of California, San Francisco 94143, USA.

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.

PMID:
10617199
DOI:
10.1038/45483
[Indexed for MEDLINE]

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