5mw0
Complex between the Leucine Zipper (LZ) and Centrosomin-motif 2 (CM2) domains of Drosophila melanogaster Centrosomin (Cnn) - L535E mutant formComplex between the Leucine Zipper (LZ) and Centrosomin-motif 2 (CM2) domains of Drosophila melanogaster Centrosomin (Cnn) - L535E mutant form
Structural highlights
FunctionCNN_DROME Core component of the centrosome throughout spermatogenesis. May participate in mitotic spindle assembly and the mechanics of morphogenesis through an interaction with microtubules, either directly or indirectly. Is a target of several homeotic genes.[1] [2] Publication Abstract from PubMedIn 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. Structural Basis for Mitotic Centrosome Assembly in Flies.,Feng Z, Caballe A, Wainman A, Johnson S, Haensele AFM, Cottee MA, Conduit PT, Lea SM, Raff JW Cell. 2017 Jun 1;169(6):1078-1089.e13. doi: 10.1016/j.cell.2017.05.030. PMID:28575671[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||