8BJS

Apo KIF20A[55-510] crystal structure

8BJS の概要

• エントリーDOI: 10.2210/pdb8bjs/pdb
• 関連するPDBエントリー: 8F18 8F1A
• EMDBエントリー: 28787 28789
• 分子名称: Kinesin-like protein KIF20A, UNK-UNK-UNK-UNK, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: kinesin 6, motor domain, atpase, mitosis, cytokinesis, golgi, microtubule, motor protein
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 52904.78

構造登録者

Ranaivoson, F.M.,Kikuti, C.,Crozet, V.,Sirkia, M.E.,Houdusse, A. (登録日: 2022-11-06, 公開日: 2023-10-04, 最終更新日: 2026-03-04)

主引用文献

Ranaivoson, F.M.,Crozet, V.,Benoit, M.P.M.H.,Abdalla Mohammed Khalid, A.,Kikuti, C.,Sirkia, H.,El Marjou, A.,Miserey-Lenkei, S.,Asenjo, A.B.,Sosa, H.,Schmidt, C.F.,Rosenfeld, S.S.,Houdusse, A.
Nucleotide-free structures of KIF20A illuminate atypical mechanochemistry in this kinesin-6.
Open Biology, 13:230122-230122, 2023

PubMed Abstract: KIF20A is a critical kinesin for cell division and a promising anti-cancer drug target. The mechanisms underlying its cellular roles remain elusive. Interestingly, unusual coupling between the nucleotide- and microtubule-binding sites of this kinesin-6 has been reported, but little is known about how its divergent sequence leads to atypical motility properties. We present here the first high-resolution structure of its motor domain that delineates the highly unusual structural features of this motor, including a long L6 insertion that integrates into the core of the motor domain and that drastically affects allostery and ATPase activity. Together with the high-resolution cryo-electron microscopy microtubule-bound KIF20A structure that reveals the microtubule-binding interface, we dissect the peculiarities of the KIF20A sequence that influence its mechanochemistry, leading to low motility compared to other kinesins. Structural and functional insights from the KIF20A pre-power stroke conformation highlight the role of extended insertions in shaping the motor's mechanochemical cycle. Essential for force production and processivity is the length of the neck linker in kinesins. We highlight here the role of the sequence preceding the neck linker in controlling its backward docking and show that a neck linker four times longer than that in kinesin-1 is required for the activity of this motor.

PubMed: 37726093
DOI: 10.1098/rsob.230122

実験手法

X-RAY DIFFRACTION (2.73 Å)