4HNA

Kinesin motor domain in the ADP-MG-ALFX state in complex with tubulin and a DARPIN

4HNA の概要

• エントリーDOI: 10.2210/pdb4hna/pdb
• 分子名称: Tubulin alpha chain, Tubulin beta chain, DESIGNED ANKYRIN REPEAT PROTEIN (DARPIN) D2, ... (10 entities in total)
• 機能のキーワード: alpha-tubulin, beta-tubulin, darpin, gtpase, kinesin, microtubule, tubulin, motor protein
• 由来する生物種: ARTIFICIAL GENE; 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton : D0VWZ0 D0VWY9 P33176
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 159175.07

構造登録者

Gigant, B.,Knossow, M. (登録日: 2012-10-19, 公開日: 2013-06-12, 最終更新日: 2023-09-20)

主引用文献

Gigant, B.,Wang, W.,Dreier, B.,Jiang, Q.,Pecqueur, L.,Pluckthun, A.,Wang, C.,Knossow, M.
Structure of a kinesin-tubulin complex and implications for kinesin motility.
Nat.Struct.Mol.Biol., 20:1001-1007, 2013

PubMed Abstract: The typical function of kinesins is to transport cargo along microtubules. Binding of ATP to microtubule-attached motile kinesins leads to cargo displacement. To better understand the nature of the conformational changes that lead to the power stroke that moves a kinesin's load along a microtubule, we determined the X-ray structure of human kinesin-1 bound to αβ-tubulin. The structure defines the mechanism of microtubule-stimulated ATP hydrolysis, which releases the kinesin motor domain from microtubules. It also reveals the structural linkages that connect the ATP nucleotide to the kinesin neck linker, a 15-amino acid segment C terminal to the catalytic core of the motor domain, to result in the power stroke. ATP binding to the microtubule-bound kinesin favors neck-linker docking. This biases the attachment of kinesin's second head in the direction of the movement, thus initiating each of the steps taken.

PubMed: 23872990
DOI: 10.1038/nsmb.2624

実験手法

X-RAY DIFFRACTION (3.19 Å)