Structure of the kinesin13-microtubule ring complex.
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.
Tan
Dongyan
D
Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx NY, 10461, USA.
Rice
William J
WJ
Sosa
Hernando
H
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D017124:Conserved Sequence; D006224:Cricetinae; D003412:Cricetulus; D029721:Drosophila Proteins / Q000737:chemistry / Q000648:ultrastructure; D004331:Drosophila melanogaster; D006801:Humans; D007091:Image Processing, Computer-Assisted; D016547:Kinesins / Q000737:chemistry* / Q000648:ultrastructure; D008870:Microtubules / Q000648:ultrastructure*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D014404:Tubulin / Q000737:chemistry* / Q000648:ultrastructure
D029721:Drosophila Proteins; D014404:Tubulin; D016547:Kinesins