Structure of the kinesin13-microtubule ring complex

Structure. 2008 Nov 12;16(11):1732-9. doi: 10.1016/j.str.2008.08.017.

Abstract

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Conserved Sequence
  • Cricetinae
  • Cricetulus
  • Drosophila Proteins / chemistry
  • Drosophila Proteins / ultrastructure
  • Drosophila melanogaster
  • Humans
  • Image Processing, Computer-Assisted
  • Kinesin / chemistry*
  • Kinesin / ultrastructure
  • Microtubules / ultrastructure*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Tubulin / chemistry*
  • Tubulin / ultrastructure

Substances

  • Drosophila Proteins
  • Tubulin
  • Kinesin

Associated data

  • PDB/3EDL