5XXT

GDP-microtubule complexed with nucleotide-free KIF5C

5XXT の概要

• エントリーDOI: 10.2210/pdb5xxt/pdb
• 関連するPDBエントリー: 5XXV 5XXW 5XXX
• EMDBエントリー: 6779 6781 6782 6783
• 分子名称: Tubulin alpha-1A chain, Tubulin beta chain, GUANOSINE-5'-TRIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: microtubule, kif5c, kinesin, structural protein
• 由来する生物種: Sus scrofa (Pig); 詳細
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 876953.03

構造登録者

Morikawa, M.,Shigematsu, H.,Nitta, R.,Hirokawa, N. (登録日: 2017-07-05, 公開日: 2018-10-10, 最終更新日: 2024-10-23)

主引用文献

Shima, T.,Morikawa, M.,Kaneshiro, J.,Kambara, T.,Kamimura, S.,Yagi, T.,Iwamoto, H.,Uemura, S.,Shigematsu, H.,Shirouzu, M.,Ichimura, T.,Watanabe, T.M.,Nitta, R.,Okada, Y.,Hirokawa, N.
Kinesin-binding-triggered conformation switching of microtubules contributes to polarized transport
J. Cell Biol., 217:4164-4183, 2018

PubMed Abstract: Kinesin-1, the founding member of the kinesin superfamily of proteins, is known to use only a subset of microtubules for transport in living cells. This biased use of microtubules is proposed as the guidance cue for polarized transport in neurons, but the underlying mechanisms are still poorly understood. Here, we report that kinesin-1 binding changes the microtubule lattice and promotes further kinesin-1 binding. This high-affinity state requires the binding of kinesin-1 in the nucleotide-free state. Microtubules return to the initial low-affinity state by washing out the binding kinesin-1 or by the binding of non-hydrolyzable ATP analogue AMPPNP to kinesin-1. X-ray fiber diffraction, fluorescence speckle microscopy, and second-harmonic generation microscopy, as well as cryo-EM, collectively demonstrated that the binding of nucleotide-free kinesin-1 to GDP microtubules changes the conformation of the GDP microtubule to a conformation resembling the GTP microtubule.

PubMed: 30297389
DOI: 10.1083/jcb.201711178

実験手法

ELECTRON MICROSCOPY (5.35 Å)