3J2U

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

3J2U の概要

• エントリーDOI: 10.2210/pdb3j2u/pdb
• EMDBエントリー: 5565
• 分子名称: Kinesin-like protein Klp10A, Tubulin alpha-1A chain, Tubulin beta-2B chain (3 entities in total)
• 機能のキーワード: tubulin, kinesin, kinesin-13, kini, depolymerase, depolymerization, microtubule, kinesin13, motor protein
• 由来する生物種: Drosophila melanogaster (Fruit fly); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 241840.93

構造登録者

Asenjo, A.B.,Chatterjee, C.,Tan, D.,DePaoli, V.,Rice, W.J.,Diaz-Avalos, R.,Silvestry, M.,Sosa, H. (登録日: 2013-01-10, 公開日: 2013-03-06, 最終更新日: 2024-02-21)

主引用文献

Asenjo, A.B.,Chatterjee, C.,Tan, D.,Depaoli, V.,Rice, W.J.,Diaz-Avalos, R.,Silvestry, M.,Sosa, H.
Structural model for tubulin recognition and deformation by Kinesin-13 microtubule depolymerases.
Cell Rep, 3:759-768, 2013

PubMed Abstract: 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.

PubMed: 23434508
DOI: 10.1016/j.celrep.2013.01.030

実験手法

ELECTRON MICROSCOPY (10.8 Å)