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5MWE

Complex between the Leucine Zipper (LZ, residues 490-567) and Centrosomin-motif 2 (CM2) domains of Drosophila melanogaster Centrosomin (Cnn)

Summary for 5MWE
Entry DOI10.2210/pdb5mwe/pdb
DescriptorCentrosomin, ZINC ION, 1,2-ETHANEDIOL, ... (6 entities in total)
Functional Keywordscentrosome, centriole, coiled-coil, mitosis, cell cycle
Biological sourceDrosophila melanogaster (Fruit fly)
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Cellular locationCytoplasm: P54623 P54623
Total number of polymer chains4
Total formula weight35073.48
Authors
Feng, Z.,Johnson, S.,Raff, J.W.,Lea, S.M. (deposition date: 2017-01-18, release date: 2017-06-28, Last modification date: 2024-05-08)
Primary citationFeng, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.02 Å)
Structure validation

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