6B0L

KLP10A-AMPPNP in complex with a microtubule

6B0L の概要

• エントリーDOI: 10.2210/pdb6b0l/pdb
• EMDBエントリー: 7026 7027 7028
• 分子名称: Tubulin alpha-1B chain, Tubulin beta chain, Kinesin-like protein Klp10A, ... (8 entities in total)
• 機能のキーワード: kinesin 13, microtubule, tubulin, depolymerization, motor protein-structural protein complex, motor protein/structural protein
• 由来する生物種: Drosophila melanogaster (Fruit fly); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 149555.18

構造登録者

Benoit, M.P.M.H.,Asenjo, A.B.,Sosa, H. (登録日: 2017-09-14, 公開日: 2018-05-02, 最終更新日: 2024-03-13)

主引用文献

Benoit, M.P.M.H.,Asenjo, A.B.,Sosa, H.
Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s.
Nat Commun, 9:1662-1662, 2018

PubMed Abstract: Kinesin-13s constitute a distinct group within the kinesin superfamily of motor proteins that promote microtubule depolymerization and lack motile activity. The molecular mechanism by which kinesin-13s depolymerize microtubules and are adapted to perform a seemingly very different activity from other kinesins is still unclear. To address this issue, here we report the near atomic resolution cryo-electron microscopy (cryo-EM) structures of Drosophila melanogaster kinesin-13 KLP10A protein constructs bound to curved or straight tubulin in different nucleotide states. These structures show how nucleotide induced conformational changes near the catalytic site are coupled with movement of the kinesin-13-specific loop-2 to induce tubulin curvature leading to microtubule depolymerization. The data highlight a modular structure that allows similar kinesin core motor-domains to be used for different functions, such as motility or microtubule depolymerization.

PubMed: 29695795
DOI: 10.1038/s41467-018-04044-8

実験手法

ELECTRON MICROSCOPY (3.98 Å)