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A model for the microtubule-Ncd motor pr ... n microscopy and image analysis
A model for the microtubule-Ncd motor protein complex obtained by cryo-electron microscopy and image analysis.
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Kinesin motors convert chemical energy from ATP hydrolysis into unidirectional movement. To understand how kinesin motors bind to and move along microtubules, we fit the atomic structure of the motor domain of Ncd (a kinesin motor involved in meiosis and mitosis) into three-dimensional density maps of Ncd-microtubule complexes calculated by cryo-electron microscopy and image analysis. The model reveals that Ncd shares an extensive interaction surface with the microtubule, and that a portion of the binding site involves loops that contain conserved residues. In the Ncd dimer, the microtubule-bound motor domain makes intimate contact with its partner head, which is dissociated from the microtubule. This head-head interaction may be important in positioning the dissociated head to take a step to the next binding site on the microtubule protofilament.
Sosa H, Dias DP, Hoenger A, Whittaker M, Wilson-Kubalek E, Sablin E, Fletterick RJ, Vale RD, Milligan RA
Cell
1997-07-25 00:00
90
2
217-24
Adenosine Triphosphatases,Animals,Cattle,Dimerization,Drosophila Proteins,Image Processing, Computer-Assisted,Kinesin,Microscopy, Electron,Microtubule Proteins,Microtubules,Protein Conformation,Protein Structure, Tertiary,X-Ray Diffraction,Drosophila Proteins,Microtubule Proteins,ncd protein, Drosophila,Adenosine Triphosphatases,Kinesin
Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92037, USA
Cell
NIAMS AR42895, NIGMS GM52468
0092-8674
S0092-8674(00)80330-X
539
True
9244296
