3WRD

Crystal Structure of the KIF5C Motor Domain Without Any Nucleotide

3WRD の概要

• エントリーDOI: 10.2210/pdb3wrd/pdb
• 分子名称: Kinesin heavy chain isoform 5C, SULFATE ION (3 entities in total)
• 機能のキーワード: kinesin, motor domain, nucleotide-free, motor protein, atpase, nucleotide binding, microtubule, transport protein
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Cytoplasm, cytoskeleton : P28738
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 76703.23

構造登録者

Inoue, S.,Nitta, R.,Hirokawa, N. (登録日: 2014-02-21, 公開日: 2015-04-01, 最終更新日: 2023-11-08)

主引用文献

Morikawa, M.,Yajima, H.,Nitta, R.,Inoue, S.,Ogura, T.,Sato, C.,Hirokawa, N.
X-ray and Cryo-EM structures reveal mutual conformational changes of Kinesin and GTP-state microtubules upon binding
Embo J., 34:1270-1286, 2015

PubMed Abstract: The molecular motor kinesin moves along microtubules using energy from ATP hydrolysis in an initial step coupled with ADP release. In neurons, kinesin-1/KIF5C preferentially binds to the GTP-state microtubules over GDP-state microtubules to selectively enter an axon among many processes; however, because the atomic structure of nucleotide-free KIF5C is unavailable, its molecular mechanism remains unresolved. Here, the crystal structure of nucleotide-free KIF5C and the cryo-electron microscopic structure of nucleotide-free KIF5C complexed with the GTP-state microtubule are presented. The structures illustrate mutual conformational changes induced by interaction between the GTP-state microtubule and KIF5C. KIF5C acquires the 'rigor conformation', where mobile switches I and II are stabilized through L11 and the initial portion of the neck-linker, facilitating effective ADP release and the weak-to-strong transition of KIF5C microtubule affinity. Conformational changes to tubulin strengthen the longitudinal contacts of the GTP-state microtubule in a similar manner to GDP-taxol microtubules. These results and functional analyses provide the molecular mechanism of the preferential binding of KIF5C to GTP-state microtubules.

PubMed: 25777528
DOI: 10.15252/embj.201490588

実験手法

X-RAY DIFFRACTION (2.86 Å)