3PYI

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

3PYI の概要

• エントリーDOI: 10.2210/pdb3pyi/pdb
• 分子名称: Spindle assembly abnormal protein 6, TETRAETHYLENE GLYCOL, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total)
• 機能のキーワード: beta-sandwich, dimer, alpha-beta protein, structural protein, cytoplasmic, centriolar
• 由来する生物種: Caenorhabditis elegans (nematode)
• 細胞内の位置: Cytoplasm: O62479
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39848.63

構造登録者

Vakonakis, I.,Steinmetz, M.O. (登録日: 2010-12-13, 公開日: 2011-02-09, 最終更新日: 2024-02-21)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.104 Å)