Large conformational changes in a kinesin motor catalyzed by interaction with microtubules.

@article{Hirose2006LargeCC,
  title={Large conformational changes in a kinesin motor catalyzed by interaction with microtubules.},
  author={Keiko Hirose and Erika Akimaru and Toshihiko Akiba and Sharyn A. Endow and Linda A Amos},
  journal={Molecular cell},
  year={2006},
  volume={23 6},
  pages={
          913-23
        }
}
Kinesin motor proteins release nucleotide upon interaction with microtubules (MTs), then bind and hydrolyze ATP to move along the MT. Although crystal structures of kinesin motors bound to nucleotides have been solved, nucleotide-free structures have not. Here, using cryomicroscopy and three-dimensional (3D) reconstruction, we report the structure of MTs decorated with a Kinesin-14 motor, Kar3, in the nucleotide-free state, as well as with ADP and AMPPNP, with resolution sufficient to show… CONTINUE READING
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