3edl

Kinesin13-Microtubule Ring complexKinesin13-Microtubule Ring complex

3edl, resolution 28.00Å Show:Asymmetric Unit Biological Assembly Structural highlights 3edl is a 5 chain structure with sequence from Bos taurus and Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Related: 1v8k, 1jff, 1sa0 Gene: DmKlp10A (DROME) Experimental data: Check Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TBA1A_PIG] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. [KIF2C_MOUSE] In complex with KIF18B, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells (By similarity). Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis (By similarity). [TBB_PIG] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structure of the kinesin13-microtubule ring complex.,Tan D, Rice WJ, Sosa H Structure. 2008 Nov 12;16(11):1732-9. PMID:19000825 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Kinesin 3D Structures Tubulin 3D Structures