3EDL

Kinesin13-Microtubule Ring complex

Summary for 3EDL

• Entry DOI: 10.2210/pdb3edl/pdb
• Related: 1jff 1sa0 1v8k
• EMDB information: 5027
• Descriptor: Tubulin alpha-1A chain, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, 2-MERCAPTO-N-[1,2,3,10-TETRAMETHOXY-9-OXO-5,6,7,9-TETRAHYDRO-BENZO[A]HEPTALEN-7-YL]ACETAMIDE, ... (12 entities in total)
• Functional Keywords: kinesin, kinesin13, kin-i, m-kinesin, microtubule, tubulin, depolymerization, structural protein
• Biological source: Drosophila melanogaster; More
• Total number of polymer chains: 5
• Total formula weight: 241021.42

Authors

Tan, D.,Rice, W.J.,Sosa, H. (deposition date: 2008-09-03, release date: 2009-01-20, Last modification date: 2024-02-21)

Primary citation

Tan, D.,Rice, W.J.,Sosa, H.
Structure of the kinesin13-microtubule ring complex.
Structure, 16:1732-1739, 2008

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 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.

PubMed: 19000825
DOI: 10.1016/j.str.2008.08.017

Experimental method

ELECTRON MICROSCOPY (28 Å)