2HXH

KIF1A head-microtubule complex structure in adp-form

2HXH の概要

• エントリーDOI: 10.2210/pdb2hxh/pdb
• 関連するPDBエントリー: 1I5S 1IA0 1JFF 2HXF
• 分子名称: Tubulin alpha chain, Tubulin beta chain, Kinesin-like protein KIF1A, ... (8 entities in total)
• 機能のキーワード: microtubule-based motor, transport protein
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 146627.99

構造登録者

Kikkawa, M.,Hirokawa, N. (登録日: 2006-08-03, 公開日: 2006-10-10, 最終更新日: 2024-06-05)

主引用文献

Kikkawa, M.,Hirokawa, N.
High-resolution cryo-EM maps show the nucleotide binding pocket of KIF1A in open and closed conformations
Embo J., 25:4187-4194, 2006

PubMed Abstract: Kinesin is an ATP-driven microtubule (MT)-based motor fundamental to organelle transport. Although a number of kinesin crystal structures have been solved, the structural evidence for coupling between the bound nucleotide and the conformation of kinesin is elusive. In addition, the structural basis of the MT-induced ATPase activity of kinesin is not clear because of the absence of the MT in the structure. Here, we report cryo-electron microscopy structures of the monomeric kinesin KIF1A-MT complex in two nucleotide states at about 10 A resolution, sufficient to reveal the secondary structure. These high-resolution maps visualized clear structural changes that suggest a mechanical pathway from the nucleotide to the neck linker via the motor core rotation. In addition, new nucleotide binding pocket conformations are observed that are different from X-ray crystallographic structures; it is closed in the 5'-adenylyl-imidodiphosphate state, but open in the ADP state. These results suggest a structural model of biased diffusion movement of monomeric kinesin motor.

PubMed: 16946706
DOI: 10.1038/sj.emboj.7601299

実験手法

ELECTRON MICROSCOPY (11 Å)