4.7 Article

Structure of the Kinesin13-Microtubule Ring Complex

Journal

STRUCTURE
Volume 16, Issue 11, Pages 1732-1739

Publisher

CELL PRESS
DOI: 10.1016/j.str.2008.08.017

Keywords

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Funding

  1. New York State Office of Science, Technology, and Academic Research
  2. National Institutes of Health [R01-AR48620]

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To investigate the mechanism of kinesin13-induced microtubule depolymerization, we have calculated a three-dimensional (3D) map of the kinesin13-microtubule ring complex, using cryo-electron microscopy (cryo-EM) and image analysis. An atomic model of the complex was produced by docking the crystal structures of tubulin and a kinesin13 motor domain (MD) into the 3D map. The model reveals a snapshot of the depolymerization mechanism by providing a 3D view of the complex formed between the kinesin13 MD and a curved tubulin protofilament (pf). It suggests that contacts mediated by kinesin13 class-specific residues in the putative microtubule-binding site stabilize intra-dimer tubulin curvature. In addition, a tubulin-binding site on the kinesin13 MD was identified. Mutations at this class-conserved site selectively disrupt the formation of microtubule-associated ring complexes.

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