3Q0X

N-terminal coiled-coil dimer domain of C. reinhardtii SAS-6 homolog Bld12p

Summary for 3Q0X

• Entry DOI: 10.2210/pdb3q0x/pdb
• Related: 3PYI 3Q0Y
• Descriptor: Centriole protein (2 entities in total)
• Functional Keywords: centrosome protein, coiled coil mediated dimer, structural protein
• Biological source: Chlamydomonas reinhardtii
• Total number of polymer chains: 2
• Total formula weight: 51628.52

Authors

Kitagawa, D.,Vakonakis, I.,Olieric, N.,Hilbert, M.,Keller, D.,Olieric, V.,Bortfeld, M.,Erat, M.C.,Flueckiger, I.,Goenczy, P.,Steinmetz, M.O. (deposition date: 2010-12-16, release date: 2011-02-09, Last modification date: 2024-10-09)

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

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

Experimental method

X-RAY DIFFRACTION (3.02 Å)