6S8M

S. pombe microtubule decorated with Cut7 motor domain in the AMPPNP state

「5MLV」から置き換えられました

6S8M の概要

• エントリーDOI: 10.2210/pdb6s8m/pdb
• EMDBエントリー: 3527
• 分子名称: Kinesin-like protein cut7, Tubulin beta chain, Tubulin alpha-1 chain, ... (8 entities in total)
• 機能のキーワード: s. pombe, microtubule, kinesin-5, cut7 motor domain, motor protein
• 由来する生物種: Schizosaccharomyces pombe (Fission yeast); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 150945.85

構造登録者

Moores, C.A.,von Loeffelholz, O. (登録日: 2019-07-10, 公開日: 2019-08-21, 最終更新日: 2025-10-01)

主引用文献

von Loeffelholz, O.,Pena, A.,Drummond, D.R.,Cross, R.,Moores, C.A.
Cryo-EM Structure (4.5- angstrom ) of Yeast Kinesin-5-Microtubule Complex Reveals a Distinct Binding Footprint and Mechanism of Drug Resistance.
J.Mol.Biol., 431:864-872, 2019

PubMed Abstract: Kinesin-5s are microtubule-dependent motors that drive spindle pole separation during mitosis. We used cryo-electron microscopy to determine the 4.5-Å resolution structure of the motor domain of the fission yeast kinesin-5 Cut7 bound to fission yeast microtubules and explored the topology of the motor-microtubule interface and the susceptibility of the complex to drug binding. Despite their non-canonical architecture and mechanochemistry, Schizosaccharomyces pombe microtubules were stabilized by epothilone at the taxane binding pocket. The overall Cut7 footprint on the S. pombe microtubule surface is altered compared to mammalian tubulin microtubules because of their different polymer architectures. However, the core motor-microtubule interaction is tightly conserved, reflected in similar Cut7 ATPase activities on each microtubule type. AMPPNP-bound Cut7 adopts a kinesin-conserved ATP-like conformation including cover neck bundle formation. However, the Cut7 ATPase is not blocked by a mammalian-specific kinesin-5 inhibitor, consistent with the non-conserved sequence and structure of its loop5 insertion.

PubMed: 30659798
DOI: 10.1016/j.jmb.2019.01.011

実験手法

ELECTRON MICROSCOPY (4.5 Å)