4NKB

Crystal Structure of the cryptic polo box (CPB)of ZYG-1

Summary for 4NKB

• Entry DOI: 10.2210/pdb4nkb/pdb
• Related: 4G7N 4NK7
• Descriptor: Probable serine/threonine-protein kinase zyg-1, MAGNESIUM ION, 2,3-DIHYDROXY-1,4-DITHIOBUTANE, ... (5 entities in total)
• Functional Keywords: cryptic polo box, centriole biogenesis, centrosomes, transferase
• Biological source: Caenorhabditis elegans (nematode)
• Cellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome: Q9GT24
• Total number of polymer chains: 2
• Total formula weight: 52982.21

Authors

Shimanovskaya, E.,Dong, G. (deposition date: 2013-11-12, release date: 2014-08-27, Last modification date: 2024-02-28)

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

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: 24980795
DOI: 10.1016/j.str.2014.05.009

Experimental method

X-RAY DIFFRACTION (2.3 Å)