2Y5W

Crystal structure of Drosophila melanogaster kinesin-1 motor domain dimer

2Y5W の概要

• エントリーDOI: 10.2210/pdb2y5w/pdb
• 関連するPDBエントリー: 2Y65
• 分子名称: KINESIN HEAVY CHAIN, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: motor protein, microtubule associated, atpase
• 由来する生物種: DROSOPHILA MELANOGASTER (FRUIT FLY)
• 細胞内の位置: Cytoplasm, cytoskeleton (Probable): P17210
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 82673.61

構造登録者

Kaan, H.Y.K.,Hackney, D.D.,Kozielski, F. (登録日: 2011-01-18, 公開日: 2011-08-24, 最終更新日: 2023-12-20)

主引用文献

Kaan, H.Y.K.,Hackney, D.D.,Kozielski, F.
The Structure of the Kinesin-1 Motor-Tail Complex Reveals the Mechanism of Autoinhibition.
Science, 333:883-, 2011

PubMed Abstract: When not transporting cargo, kinesin-1 is autoinhibited by binding of a tail region to the motor domains, but the mechanism of inhibition is unclear. We report the crystal structure of a motor domain dimer in complex with its tail domain at 2.2 angstroms and compare it with a structure of the motor domain alone at 2.7 angstroms. These structures indicate that neither an induced conformational change nor steric blocking is the cause of inhibition. Instead, the tail cross-links the motor domains at a second position, in addition to the coiled coil. This "double lockdown," by cross-linking at two positions, prevents the movement of the motor domains that is needed to undock the neck linker and release adenosine diphosphate. This autoinhibition mechanism could extend to some other kinesins.

PubMed: 21836017
DOI: 10.1126/SCIENCE.1204824

実験手法

X-RAY DIFFRACTION (2.7 Å)