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-Structure paper
Title | Structure of the kinesin13-microtubule ring complex. |
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Journal, issue, pages | Structure, Vol. 16, Issue 11, Page 1732-1739, Year 2008 |
Publish date | Nov 12, 2008 |
![]() | Dongyan Tan / William J Rice / Hernando Sosa / ![]() |
PubMed 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 ...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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Methods | EM (helical sym.) |
Resolution | 28.0 Å |
Structure data | |
Chemicals | ![]() ChemComp-ZN: ![]() ChemComp-MG: ![]() ChemComp-GTP: ![]() ChemComp-GDP: ![]() ChemComp-TA1: ![]() ChemComp-ANP: ![]() ChemComp-CN2: ![]() ChemComp-HOH: |
Source |
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![]() | STRUCTURAL PROTEIN / Kinesin / Kinesin13 / Kin-I / M-Kinesin / Microtubule / Tubulin / depolymerization |