9JKB

Cryo-EM structure of the CUL1-RBX1-SKP1-FBXO4 SCF ubiquition ligase complex

9JKB の概要

• エントリーDOI: 10.2210/pdb9jkb/pdb
• EMDBエントリー: 61550
• 分子名称: F-box only protein 4, Cullin-1, S-phase kinase-associated protein 1, ... (4 entities in total)
• 機能のキーワード: ubiquitination e3 ligase, cryo-em, protein binding
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 194287.62

構造登録者

Zhu, W.,Xu, C. (登録日: 2024-09-15, 公開日: 2024-10-23, 最終更新日: 2024-10-30)

主引用文献

Zhu, W.,Chen, X.,Zhang, J.,Xu, C.
Structure of the CUL1-RBX1-SKP1-FBXO4 SCF ubiquitin ligase complex.
Biochem.Biophys.Res.Commun., 735:150811-150811, 2024

PubMed Abstract: Cullin-RING E3 ubiquitin ligases (CRLs) constitute the largest family of ubiquitin ligase and play important roles in regulation of proteostasis. Here we presented the cryo-EM structure of CRL1, a member of Cullin-1 E3 ligase. CRL1 adopts a homodimer architecture. Structural analysis revealed that in the CRL1 protomer, the substrate recognition subunit FBXO4 interacts both the adaptor protein SKP1, and the scaffold protein CUL1 via hydrophobic and electrostatic interactions. Two FBXO4 forms a domain-swapped dimer in the CRL1 structure, which constitutes the basis for the dimerization of CRL1. Inspired by the cryo-EM density, we modeled the architecture of whole CRL1 as a symmetrical dimer, which provides insights into CRL1-medaited turnover of oncogene proteins.

PubMed: 39406020
DOI: 10.1016/j.bbrc.2024.150811

実験手法

ELECTRON MICROSCOPY (3.93 Å)