5GSZ

Crystal Structure of the KIF19A Motor Domain Complexed with Mg-ADP

5GSZ の概要

• エントリーDOI: 10.2210/pdb5gsz/pdb
• 分子名称: Kinesin-like protein KIF19, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: kinesin, motor domain, mg-adp, motor protein
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40120.52

構造登録者

Wang, D.,Nitta, R.,Hirokawa, N. (登録日: 2016-08-18, 公開日: 2016-09-28, 最終更新日: 2024-10-16)

主引用文献

Wang, D.,Nitta, R.,Morikawa, M.,Yajima, H.,Inoue, S.,Shigematsu, H.,Kikkawa, M.,Hirokawa, N.
Motility and microtubule depolymerization mechanisms of the Kinesin-8 motor, KIF19A
Elife, 5:-, 2016

PubMed Abstract: The kinesin-8 motor, KIF19A, accumulates at cilia tips and controls cilium length. Defective KIF19A leads to hydrocephalus and female infertility because of abnormally elongated cilia. Uniquely among kinesins, KIF19A possesses the dual functions of motility along ciliary microtubules and depolymerization of microtubules. To elucidate the molecular mechanisms of these functions we solved the crystal structure of its motor domain and determined its cryo-electron microscopy structure complexed with a microtubule. The features of KIF19A that enable its dual function are clustered on its microtubule-binding side. Unexpectedly, a destabilized switch II coordinates with a destabilized L8 to enable KIF19A to adjust to both straight and curved microtubule protofilaments. The basic clusters of L2 and L12 tether the microtubule. The long L2 with a characteristic acidic-hydrophobic-basic sequence effectively stabilizes the curved conformation of microtubule ends. Hence, KIF19A utilizes multiple strategies to accomplish the dual functions of motility and microtubule depolymerization by ATP hydrolysis.

PubMed: 27690357
DOI: 10.7554/eLife.18101

実験手法

X-RAY DIFFRACTION (2.72 Å)