3Q0X: N-Terminal Coiled-Coil Dimer Domain Of C. Reinhardtii Sas-6 Homolog Bld12p

Citation:
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.
PDB ID: 3Q0XDownload
MMDB ID: 88577
PDB Deposition Date: 2010/12/16
Updated in MMDB: 2011/05
Experimental Method:
x-ray diffraction
Resolution: 3.02  Å
Source Organism:
Similar Structures:
Biological Unit for 3Q0X: dimeric; determined by author and by software (PISA)
Molecular Components in 3Q0X
Label Count Molecule
Proteins (2 molecules)
2
Centriole Protein
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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