3Q0X
N-terminal coiled-coil dimer domain of C. reinhardtii SAS-6 homolog Bld12p
3Q0X の概要
エントリーDOI | 10.2210/pdb3q0x/pdb |
関連するPDBエントリー | 3PYI 3Q0Y |
分子名称 | Centriole protein (2 entities in total) |
機能のキーワード | centrosome protein, coiled coil mediated dimer, structural protein |
由来する生物種 | Chlamydomonas reinhardtii |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 51628.52 |
構造登録者 | Kitagawa, D.,Vakonakis, I.,Olieric, N.,Hilbert, M.,Keller, D.,Olieric, V.,Bortfeld, M.,Erat, M.C.,Flueckiger, I.,Goenczy, P.,Steinmetz, M.O. (登録日: 2010-12-16, 公開日: 2011-02-09, 最終更新日: 2024-10-09) |
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 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 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.02 Å) |
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