A structural change in the kinesin motor protein that drives motility.
Autor: | Rice S; Department of Cellular and Molecular Pharmacology, University of California, San Francisco 94143, USA., Lin AW, Safer D, Hart CL, Naber N, Carragher BO, Cain SM, Pechatnikova E, Wilson-Kubalek EM, Whittaker M, Pate E, Cooke R, Taylor EW, Milligan RA, Vale RD |
---|---|
Jazyk: | angličtina |
Zdroj: | Nature [Nature] 1999 Dec 16; Vol. 402 (6763), pp. 778-84. |
DOI: | 10.1038/45483 |
Abstrakt: | 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. |
Databáze: | MEDLINE |
Externí odkaz: |
načítá se...