5HNW

Structural basis of backwards motion in kinesin-14: minus-end directed nKn664 in the AMPPNP state

5HNW の概要

• エントリーDOI: 10.2210/pdb5hnw/pdb
• EMDBエントリー: 8058
• 分子名称: Tubulin alpha-1B chain, Tubulin beta-2B chain, Protein claret segregational,KINESIN HEAVY CHAIN ISOFORM 5C, ... (8 entities in total)
• 機能のキーワード: kinesin, kinesin-14, microtubule, atpase, transport protein
• 由来する生物種: Drosophila melanogaster (Fruit fly); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 143747.96

構造登録者

Shigematsu, H.,Yokoyama, T.,Kikkawa, M.,Shirouzu, M.,Nitta, R. (登録日: 2016-01-19, 公開日: 2016-08-10, 最終更新日: 2024-10-09)

主引用文献

Yamagishi, M.,Shigematsu, H.,Yokoyama, T.,Kikkawa, M.,Sugawa, M.,Aoki, M.,Shirouzu, M.,Yajima, J.,Nitta, R.
Structural Basis of Backwards Motion in Kinesin-1-Kinesin-14 Chimera: Implication for Kinesin-14 Motility
Structure, 24:1322-1334, 2016

PubMed Abstract: Kinesin-14 is a unique minus-end-directed microtubule-based motor. A swinging motion of a class-specific N-terminal neck helix has been proposed to produce minus-end directionality. However, it is unclear how swinging of the neck helix is driven by ATP hydrolysis utilizing the highly conserved catalytic core among all kinesins. Here, using a motility assay, we show that in addition to the neck helix, the conserved five residues at the C-terminal region in kinesin-14, namely the neck mimic, are necessary to give kinesin-1 an ability to reverse its directionality toward the minus end of microtubules. Our structural analyses further demonstrate that the C-terminal neck mimic, in cooperation with conformational changes in the catalytic core during ATP binding, forms a kinesin-14 bundle with the N-terminal neck helix to swing toward the minus end of microtubules. Thus, the neck mimic plays a crucial role in coupling the chemical ATPase reaction with the mechanical cycle to produce the minus-end-directed motility of kinesin-14.

PubMed: 27452403
DOI: 10.1016/j.str.2016.05.021

実験手法

ELECTRON MICROSCOPY (6.6 Å)