A structural change in the kinesin motor protein that drives motility |
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Authors: | Rice S Lin A W Safer D Hart C L Naber N Carragher B O Cain S M Pechatnikova E Wilson-Kubalek E M Whittaker M Pate E Cooke R Taylor E W Milligan R A Vale R D |
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Affiliation: | Department of Cellular and Molecular Pharmacology, University of California, San Francisco 94143, USA. |
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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. |
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