TY - JOUR
T1 - A model for the microtubule-Ncd motor protein complex obtained by cryo- electron microscopy and image analysis
AU - Sosa, Hernando
AU - Prabha Dias, D.
AU - Hoenger, Andreas
AU - Whittaker, Michael
AU - Wilson-Kubalek, Elizabeth
AU - Sablin, Elena
AU - Fletterick, Robert J.
AU - Vale, Ronald D.
AU - Milligan, Ronald A.
N1 - Funding Information:
We thank Bridget Carragher for help with computer programs. This work was supported by grants from the National Institutes of Health (GM52468 to R. A. M. and AR42895 to R. J. F. and R. D. V.), a Human Frontier Science Program Fellowship (LT-619/94 to A. H.), a Leukemia Society of America postdoctoral fellowship (to E. S.), and an American Heart Association predoctoral fellowship (to D. P. D.). R. A. M. is an Established Investigator of the American Heart Association.
PY - 1997/7/25
Y1 - 1997/7/25
N2 - 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.
AB - 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.
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U2 - 10.1016/S0092-8674(00)80330-X
DO - 10.1016/S0092-8674(00)80330-X
M3 - Article
C2 - 9244296
AN - SCOPUS:0343811700
SN - 0092-8674
VL - 90
SP - 217
EP - 224
JO - Cell
JF - Cell
IS - 2
ER -