9JKB

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

Summary for 9JKB

• Entry DOI: 10.2210/pdb9jkb/pdb
• EMDB information: 61550
• Descriptor: F-box only protein 4, Cullin-1, S-phase kinase-associated protein 1, ... (4 entities in total)
• Functional Keywords: ubiquitination e3 ligase, cryo-em, protein binding
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 5
• Total formula weight: 194287.62

Authors

Zhu, W.,Xu, C. (deposition date: 2024-09-15, release date: 2024-10-23, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3.93 Å)