3j2u | pdb_00003j2u

Kinesin-13 KLP10A HD in complex with CS-tubulin and a microtubule

spinqualitylabelsall models 3j2u, resolution 10.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3j2u is a 5 chain structure with sequence from Bos taurus and Drome. The July 2014 RCSB PDB Molecule of the Month feature on Microtubules by David Goodsell is 10.2210/rcsb_pdb/mom_2014_7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: Klp10A, CG1453 (DROME) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [KI10A_DROME] Required during anaphase to drive sister chromatid separation to promote flux by actively depolymerizing kinetochore microtubules at their pole-associated minus ends, thereby moving chromatids through a "poleward flux". [TBB2B_BOVIN] 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 (By similarity). [TBA1B_BOVIN] 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. Publication Abstract from PubMed To elucidate the structural basis of the mechanism of microtubule depolymerization by kinesin-13s, we analyzed complexes of tubulin and the Drosophila melanogaster kinesin-13 KLP10A by electron microscopy (EM) and fluorescence polarization microscopy. We report a nanometer-resolution (1.1 nm) cryo-EM three-dimensional structure of the KLP10A head domain (KLP10AHD) bound to curved tubulin. We found that binding of KLP10AHD induces a distinct tubulin configuration with displacement (shear) between tubulin subunits in addition to curvature. In this configuration, the kinesin-binding site differs from that in straight tubulin, providing an explanation for the distinct interaction modes of kinesin-13s with the microtubule lattice or its ends. The KLP10AHD-tubulin interface comprises three areas of interaction, suggesting a crossbow-type tubulin-bending mechanism. These areas include the kinesin-13 family conserved KVD residues, and as predicted from the crossbow model, mutating these residues changes the orientation and mobility of KLP10AHDs interacting with the microtubule. Structural Model for Tubulin Recognition and Deformation by Kinesin-13 Microtubule Depolymerases.,Asenjo AB, Chatterjee C, Tan D, Depaoli V, Rice WJ, Diaz-Avalos R, Silvestry M, Sosa H Cell Rep. 2013 Feb 19. pii: S2211-1247(13)00054-5. doi:, 10.1016/j.celrep.2013.01.030. PMID:23434508 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tubulin

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