5ND4

Microtubule-bound MKLP2 motor domain in the presence of ADP.AlFx

5ND4 の概要

• エントリーDOI: 10.2210/pdb5nd4/pdb
• EMDBエントリー: 3622
• 分子名称: Kinesin-like protein KIF20A, Tubulin alpha chain, Tubulin beta-2B chain, ... (9 entities in total)
• 機能のキーワード: kinesin, mitosis, microtubules, motor protein
• 由来する生物種: Mus musculus (House Mouse); 詳細
• 細胞内の位置: Golgi apparatus : P97329; Cytoplasm, cytoskeleton : F2Z4C1 Q6B856
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 152190.13

構造登録者

Atherton, J.,Yu, I.-M.,Cook, A.,Muretta, J.M.,Joseph, A.P.,Major, J.,Sourigues, Y.,Clause, J.,Topf, M.,Rosenfeld, S.S.,Houdusse, A.,Moores, C.A. (登録日: 2017-03-07, 公開日: 2017-10-04, 最終更新日: 2024-05-15)

主引用文献

Atherton, J.,Yu, I.M.,Cook, A.,Muretta, J.M.,Joseph, A.,Major, J.,Sourigues, Y.,Clause, J.,Topf, M.,Rosenfeld, S.S.,Houdusse, A.,Moores, C.A.
The divergent mitotic kinesin MKLP2 exhibits atypical structure and mechanochemistry.
Elife, 6:-, 2017

PubMed Abstract: MKLP2, a kinesin-6, has critical roles during the metaphase-anaphase transition and cytokinesis. Its motor domain contains conserved nucleotide binding motifs, but is divergent in sequence (~35% identity) and size (~40% larger) compared to other kinesins. Using cryo-electron microscopy and biophysical assays, we have undertaken a mechanochemical dissection of the microtubule-bound MKLP2 motor domain during its ATPase cycle, and show that many facets of its mechanism are distinct from other kinesins. While the MKLP2 neck-linker is directed towards the microtubule plus-end in an ATP-like state, it does not fully dock along the motor domain. Furthermore, the footprint of the MKLP2 motor domain on the MT surface is altered compared to motile kinesins, and enhanced by kinesin-6-specific sequences. The conformation of the highly extended loop6 insertion characteristic of kinesin-6s is nucleotide-independent and does not contact the MT surface. Our results emphasize the role of family-specific insertions in modulating kinesin motor function.

PubMed: 28826477
DOI: 10.7554/eLife.27793

実験手法

ELECTRON MICROSCOPY (4.4 Å)