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-Structure paper
タイトル | Structure of the kinesin13-microtubule ring complex. |
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ジャーナル・号・ページ | Structure, Vol. 16, Issue 11, Page 1732-1739, Year 2008 |
掲載日 | 2008年11月12日 |
著者 | Dongyan Tan / William J Rice / Hernando Sosa / |
PubMed 要旨 | 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. |
リンク | Structure / PubMed:19000825 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 28.0 Å |
構造データ | |
化合物 | ChemComp-ZN: ChemComp-MG: ChemComp-GTP: ChemComp-GDP: ChemComp-TA1: ChemComp-ANP: ChemComp-CN2: ChemComp-HOH: |
由来 |
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キーワード | STRUCTURAL PROTEIN / Kinesin / Kinesin13 / Kin-I / M-Kinesin / Microtubule / Tubulin / depolymerization |