7EQB

Crystal structure of the dimerization domain of ZEN-4

Summary for 7EQB

• Entry DOI: 10.2210/pdb7eqb/pdb
• Descriptor: Kinesin-like protein, SULFATE ION (3 entities in total)
• Functional Keywords: zen-4, dimerization domain, coiled-coil, cell cycle
• Biological source: Caenorhabditis elegans
• Total number of polymer chains: 2
• Total formula weight: 18837.43

Authors

Chen, Z.,Pan, H. (deposition date: 2021-05-01, release date: 2022-04-13, Last modification date: 2024-05-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.103 Å)