7LVQ

KIF14[391-743] - AMP-PNP closed state class in complex with a microtubule

7LVQ の概要

• エントリーDOI: 10.2210/pdb7lvq/pdb
• EMDBエントリー: 23540 23541
• 分子名称: Tubulin alpha-1B chain, Tubulin beta-2B chain, Kinesin-like protein KIF14, ... (8 entities in total)
• 機能のキーワード: kif14, kinesin, motility, microtubule, tubulin, motor protein
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 142331.15

構造登録者

Benoit, M.P.M.H.,Asenjo, A.B.,Paydar, M.,Dhakal, S.,Kwok, B.,Sosa, H. (登録日: 2021-02-26, 公開日: 2021-05-05, 最終更新日: 2024-03-06)

主引用文献

Benoit, M.P.M.H.,Asenjo, A.B.,Paydar, M.,Dhakal, S.,Kwok, B.H.,Sosa, H.
Structural basis of mechano-chemical coupling by the mitotic kinesin KIF14.
Nat Commun, 12:3637-3637, 2021

PubMed Abstract: KIF14 is a mitotic kinesin whose malfunction is associated with cerebral and renal developmental defects and several cancers. Like other kinesins, KIF14 couples ATP hydrolysis and microtubule binding to the generation of mechanical work, but the coupling mechanism between these processes is still not fully clear. Here we report 20 high-resolution (2.7-3.9 Å) cryo-electron microscopy KIF14-microtubule structures with complementary functional assays. Analysis procedures were implemented to separate coexisting conformations of microtubule-bound monomeric and dimeric KIF14 constructs. The data provide a comprehensive view of the microtubule and nucleotide induced KIF14 conformational changes. It shows that: 1) microtubule binding, the nucleotide species, and the neck-linker domain govern the transition between three major conformations of the motor domain; 2) an undocked neck-linker prevents the nucleotide-binding pocket to fully close and dampens ATP hydrolysis; 3) 13 neck-linker residues are required to assume a stable docked conformation; 4) the neck-linker position controls the hydrolysis rather than the nucleotide binding step; 5) the two motor domains of KIF14 dimers adopt distinct conformations when bound to the microtubule; and 6) the formation of the two-heads-bound-state introduces structural changes in both motor domains of KIF14 dimers. These observations provide the structural basis for a coordinated chemo-mechanical kinesin translocation model.

PubMed: 34131133
DOI: 10.1038/s41467-021-23581-3

実験手法

ELECTRON MICROSCOPY (2.9 Å)