3PYI
Structure of the N-terminal domain of C. elegans SAS-6
Summary for 3PYI
| Entry DOI | 10.2210/pdb3pyi/pdb |
| Descriptor | Spindle assembly abnormal protein 6, TETRAETHYLENE GLYCOL, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total) |
| Functional Keywords | beta-sandwich, dimer, alpha-beta protein, structural protein, cytoplasmic, centriolar |
| Biological source | Caenorhabditis elegans (nematode) |
| Cellular location | Cytoplasm: O62479 |
| Total number of polymer chains | 2 |
| Total formula weight | 39848.63 |
| Authors | Vakonakis, I.,Steinmetz, M.O. (deposition date: 2010-12-13, release date: 2011-02-09, Last modification date: 2024-02-21) |
| Primary citation | Kitagawa, D.,Vakonakis, I.,Olieric, N.,Hilbert, M.,Keller, D.,Olieric, V.,Bortfeld, M.,Erat, M.C.,Fluckiger, I.,Gonczy, P.,Steinmetz, M.O. Structural basis of the 9-fold symmetry of centrioles. Cell(Cambridge,Mass.), 144:364-375, 2011 Cited by PubMed Abstract: The centriole, and the related basal body, is an ancient organelle characterized by a universal 9-fold radial symmetry and is critical for generating cilia, flagella, and centrosomes. The mechanisms directing centriole formation are incompletely understood and represent a fundamental open question in biology. Here, we demonstrate that the centriolar protein SAS-6 forms rod-shaped homodimers that interact through their N-terminal domains to form oligomers. We establish that such oligomerization is essential for centriole formation in C. elegans and human cells. We further generate a structural model of the related protein Bld12p from C. reinhardtii, in which nine homodimers assemble into a ring from which nine coiled-coil rods radiate outward. Moreover, we demonstrate that recombinant Bld12p self-assembles into structures akin to the central hub of the cartwheel, which serves as a scaffold for centriole formation. Overall, our findings establish a structural basis for the universal 9-fold symmetry of centrioles. PubMed: 21277013DOI: 10.1016/j.cell.2011.01.008 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.104 Å) |
Structure validation
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