5I7C

Centrosomin-motif 2 (CM2) domain of Drosophila melanogaster Centrosomin (Cnn)

Summary for 5I7C

• Entry DOI: 10.2210/pdb5i7c/pdb
• Descriptor: Centrosomin, ZINC ION (2 entities in total)
• Functional Keywords: non-canonical-coiled-coil, centrosome, pcm, zinc-binding, structural protein
• Biological source: Drosophila melanogaster (Fruit fly)
• Cellular location: Cytoplasm: P54623
• Total number of polymer chains: 4
• Total formula weight: 32924.53

Authors

Feng, Z.,Cottee, M.A.,Johnson, S.,Lea, S.M. (deposition date: 2016-02-17, release date: 2017-03-08, Last modification date: 2024-05-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.804 Å)