6CSV

The structure of the Cep63-Cep152 heterotetrameric complex

6CSV の概要

• エントリーDOI: 10.2210/pdb6csv/pdb
• 分子名称: Centrosomal protein of 63 kDa,Centrosomal protein of 152 kDa (2 entities in total)
• 機能のキーワード: centrosome, complex, hydrophobic, cell cycle
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 44354.86

構造登録者

Lee, E.,Chen, Y.,Zhang, L.,Kim, T.S.,Ahn, J.I.,Park, J.E.,Lee, K.S. (登録日: 2018-03-21, 公開日: 2019-03-27, 最終更新日: 2024-03-13)

主引用文献

Kim, T.S.,Zhang, L.,Il Ahn, J.,Meng, L.,Chen, Y.,Lee, E.,Bang, J.K.,Lim, J.M.,Ghirlando, R.,Fan, L.,Wang, Y.X.,Kim, B.Y.,Park, J.E.,Lee, K.S.
Molecular architecture of a cylindrical self-assembly at human centrosomes.
Nat Commun, 10:1151-1151, 2019

PubMed Abstract: The cell is constructed by higher-order structures and organelles through complex interactions among distinct structural constituents. The centrosome is a membraneless organelle composed of two microtubule-derived structures called centrioles and an amorphous mass of pericentriolar material. Super-resolution microscopic analyses in various organisms revealed that diverse pericentriolar material proteins are concentrically localized around a centriole in a highly organized manner. However, the molecular nature underlying these organizations remains unknown. Here we show that two human pericentriolar material scaffolds, Cep63 and Cep152, cooperatively generate a heterotetrameric α-helical bundle that functions in conjunction with its neighboring hydrophobic motifs to self-assemble into a higher-order cylindrical architecture capable of recruiting downstream components, including Plk4, a key regulator for centriole duplication. Mutations disrupting the self-assembly abrogate Plk4-mediated centriole duplication. Because pericentriolar material organization is evolutionarily conserved, this work may offer a paradigm for investigating the assembly and function of centrosomal scaffolds in various organisms.

PubMed: 30858376
DOI: 10.1038/s41467-019-08838-2

実験手法

X-RAY DIFFRACTION (2.5 Å)