7EQB

Crystal structure of the dimerization domain of ZEN-4

7EQB の概要

• エントリーDOI: 10.2210/pdb7eqb/pdb
• 分子名称: Kinesin-like protein, SULFATE ION (3 entities in total)
• 機能のキーワード: zen-4, dimerization domain, coiled-coil, cell cycle
• 由来する生物種: Caenorhabditis elegans
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18837.43

構造登録者

Chen, Z.,Pan, H. (登録日: 2021-05-01, 公開日: 2022-04-13, 最終更新日: 2024-05-29)

主引用文献

Pan, H.,Guan, R.,Zhao, R.,Ou, G.,Chen, Z.
Mechanistic insights into central spindle assembly mediated by the centralspindlin complex.
Proc.Natl.Acad.Sci.USA, 118:-, 2021

PubMed Abstract: The central spindle spatially and temporally regulates the formation of division plane during cytokinesis in animal cells. The heterotetrameric centralspindlin complex bundles microtubules to assemble the central spindle, the mechanism of which is poorly understood. Here, we determined the crystal structures of the molecular backbone of ZEN-4/CYK-4 centralspindlin from , which revealed the detailed mechanism of complex formation. The molecular backbone of centralspindlin has the intrinsic propensity to undergo liquid-liquid phase separation. The condensation of centralspindlin requires two patches of basic residues at ZEN-4 and multiple acidic residues at the intrinsically disordered region of CYK-4, explaining the synergy of the two subunits for the function. These complementary charged residues were critical for the microtubule bundling activity of centralspindlin in vitro and for the assembly of the central spindle in vivo. Together, our findings provide insights into the mechanism of central spindle assembly mediated by centralspindlin through charge-driven macromolecular condensation.

PubMed: 34588311
DOI: 10.1073/pnas.2112039118

実験手法

X-RAY DIFFRACTION (2.103 Å)