5MW9

Complex between the Leucine Zipper (LZ) and Centrosomin-motif 2 (CM2) domains of Drosophila melanogaster Centrosomin (Cnn) - L535E mutant form

5MW9 の概要

• エントリーDOI: 10.2210/pdb5mw9/pdb
• 分子名称: Centrosomin, ZINC ION, ... (4 entities in total)
• 機能のキーワード: centrosome, centriole, coiled-coil, mitosis, cell cycle
• 由来する生物種: Drosophila melanogaster (Fruit fly); 詳細
• 細胞内の位置: Cytoplasm: P54623 P54623
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 59190.17

構造登録者

Feng, Z.,Johnson, S.,Raff, J.W.,Lea, S.M. (登録日: 2017-01-18, 公開日: 2017-06-28, 最終更新日: 2024-11-20)

主引用文献

Feng, Z.,Caballe, A.,Wainman, A.,Johnson, S.,Haensele, A.F.M.,Cottee, M.A.,Conduit, P.T.,Lea, S.M.,Raff, J.W.
Structural Basis for Mitotic Centrosome Assembly in Flies.
Cell, 169:1078-1089.e13, 2017

PubMed Abstract: In flies, Centrosomin (Cnn) forms a phosphorylation-dependent scaffold that recruits proteins to the mitotic centrosome, but how Cnn assembles into a scaffold is unclear. We show that scaffold assembly requires conserved leucine zipper (LZ) and Cnn-motif 2 (CM2) domains that co-assemble into a 2:2 complex in vitro. We solve the crystal structure of the LZ:CM2 complex, revealing that both proteins form helical dimers that assemble into an unusual tetramer. A slightly longer version of the LZ can form micron-scale structures with CM2, whose assembly is stimulated by Plk1 phosphorylation in vitro. Mutating individual residues that perturb LZ:CM2 tetramer assembly perturbs the formation of these micron-scale assemblies in vitro and Cnn-scaffold assembly in vivo. Thus, Cnn molecules have an intrinsic ability to form large, LZ:CM2-interaction-dependent assemblies that are critical for mitotic centrosome assembly. These studies provide the first atomic insight into a molecular interaction required for mitotic centrosome assembly.

PubMed: 28575671
DOI: 10.1016/j.cell.2017.05.030

実験手法

X-RAY DIFFRACTION (2.2 Å)