4NK7
Crystal Structure of the D. melanogaster Plk4 cryptic polo box (CPB)
Summary for 4NK7
| Entry DOI | 10.2210/pdb4nk7/pdb |
| Related | 4G7N 4NKB |
| Descriptor | Serine/threonine-protein kinase PLK4 (1 entity in total) |
| Functional Keywords | cryptic polo box, plk4 targeting, rocentrioles, asterless n-terminus, centrosomes, transferase |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Cellular location | Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole: O97143 |
| Total number of polymer chains | 1 |
| Total formula weight | 25498.28 |
| Authors | Dong, G.,Lesigang, J. (deposition date: 2013-11-12, release date: 2014-08-27, Last modification date: 2023-09-20) |
| Primary citation | Shimanovskaya, E.,Viscardi, V.,Lesigang, J.,Lettman, M.M.,Qiao, R.,Svergun, D.I.,Round, A.,Oegema, K.,Dong, G. Structure of the C. elegans ZYG-1 Cryptic Polo Box Suggests a Conserved Mechanism for Centriolar Docking of Plk4 Kinases. Structure, 22:1090-1104, 2014 Cited by PubMed Abstract: Plk4 family kinases control centriole assembly. Plk4s target mother centrioles through an interaction between their cryptic polo box (CPB) and acidic regions in the centriolar receptors SPD-2/Cep192 and/or Asterless/Cep152. Here, we report a crystal structure for the CPB of C. elegans ZYG-1, which forms a Z-shaped dimer containing an intermolecular β sheet with an extended basic surface patch. Biochemical and in vivo analysis revealed that electrostatic interactions dock the ZYG-1 CPB basic patch onto the SPD-2-derived acidic region to promote ZYG-1 targeting and new centriole assembly. Analysis of a different crystal form of the Drosophila Plk4 (DmPlk4) CPB suggests that it also forms a Z-shaped dimer. Comparison of the ZYG-1 and DmPlk4 CPBs revealed structural changes in the ZYG-1 CPB that confer selectivity for binding SPD-2 over Asterless-derived acidic regions. Overall, our findings suggest a conserved mechanism for centriolar docking of Plk4 homologs that initiate daughter centriole assembly. PubMed: 24980795DOI: 10.1016/j.str.2014.05.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.233 Å) |
Structure validation
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