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3PYI

Structure of the N-terminal domain of C. elegans SAS-6

Summary for 3PYI
Entry DOI10.2210/pdb3pyi/pdb
DescriptorSpindle assembly abnormal protein 6, TETRAETHYLENE GLYCOL, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total)
Functional Keywordsbeta-sandwich, dimer, alpha-beta protein, structural protein, cytoplasmic, centriolar
Biological sourceCaenorhabditis elegans (nematode)
Cellular locationCytoplasm: O62479
Total number of polymer chains2
Total formula weight39848.63
Authors
Vakonakis, I.,Steinmetz, M.O. (deposition date: 2010-12-13, release date: 2011-02-09, Last modification date: 2024-02-21)
Primary citationKitagawa, 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: 21277013
DOI: 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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