A model for the microtubule-Ncd motor protein complex obtained by cryo- electron microscopy and image analysis

Hernando Sosa, D. Prabha Dias, Andreas Hoenger, Michael Whittaker, Elizabeth Wilson-Kubalek, Elena Sablin, Robert J. Fletterick, Ronald D. Vale, Ronald A. Milligan

Research output: Contribution to journalArticle

135 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)217-224
Number of pages8
JournalCell
Volume90
Issue number2
DOIs
StatePublished - Jul 25 1997
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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