A structural change in the kinesin motor protein that drives motility - PubMed (original) (raw)
. 1999 Dec 16;402(6763):778-84.
doi: 10.1038/45483.
A W Lin, D Safer, C L Hart, N Naber, B O Carragher, S M Cain, E Pechatnikova, E M Wilson-Kubalek, M Whittaker, E Pate, R Cooke, E W Taylor, R A Milligan, R D Vale
Affiliations
- PMID: 10617199
- DOI: 10.1038/45483
A structural change in the kinesin motor protein that drives motility
S Rice et al. Nature. 1999.
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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