5XJA

The Crystal Structure of the Minimal Core Domain of the Microtubule Depolymerizer KIF2C Complexed with ADP-Mg-AlFx

5XJA の概要

• エントリーDOI: 10.2210/pdb5xja/pdb
• 関連するPDBエントリー: 5XJB
• 分子名称: Kinesin-like protein KIF2C, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: kinesin, microtubule, tubulin, kif2, mcak, depolymerization, structural protein
• 由来する生物種: Mus musculus (Mouse)
• 細胞内の位置: Cytoplasm, cytoskeleton : Q922S8
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 97978.05

構造登録者

Ogawa, T.,Jiang, X.,Hirokawa, N. (登録日: 2017-04-30, 公開日: 2017-09-13, 最終更新日: 2023-11-22)

主引用文献

Ogawa, T.,Saijo, S.,Shimizu, N.,Jiang, X.,Hirokawa, N.
Mechanism of Catalytic Microtubule Depolymerization via KIF2-Tubulin Transitional Conformation
Cell Rep, 20:2626-2638, 2017

PubMed Abstract: Microtubules (MTs) are dynamic structures that are fundamental for cell morphogenesis and motility. MT-associated motors work efficiently to perform their functions. Unlike other motile kinesins, KIF2 catalytically depolymerizes MTs from the peeled protofilament end during ATP hydrolysis. However, the detailed mechanism by which KIF2 drives processive MT depolymerization remains unknown. To elucidate the catalytic mechanism, the transitional KIF2-tubulin complex during MT depolymerization was analyzed through multiple methods, including atomic force microscopy, size-exclusion chromatography, multi-angle light scattering, small-angle X-ray scattering, analytical ultracentrifugation, and mass spectrometry. The analyses outlined the conformation in which one KIF2core domain binds tightly to two tubulin dimers in the middle pre-hydrolysis state during ATP hydrolysis, a process critical for catalytic MT depolymerization. The X-ray crystallographic structure of the KIF2core domain displays the activated conformation that sustains the large KIF2-tubulin 1:2 complex.

PubMed: 28903043
DOI: 10.1016/j.celrep.2017.08.067

実験手法

X-RAY DIFFRACTION (3.43 Å)