8K8T

Structure of CUL3-RBX1-KLHL22 complex

Summary for 8K8T

• Entry DOI: 10.2210/pdb8k8t/pdb
• EMDB information: 36961 39725
• Descriptor: Cullin-3, Kelch-like protein 22 (2 entities in total)
• Functional Keywords: cullin ring e3 ubiquitin ligase, ligase
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 330225.34

Authors

Wang, W.,Ling, L.,Dai, Z.,Zuo, P.,Yin, Y. (deposition date: 2023-07-31, release date: 2024-05-22)

Primary citation

Wang, W.,Liang, L.,Dai, Z.,Zuo, P.,Yu, S.,Lu, Y.,Ding, D.,Chen, H.,Shan, H.,Jin, Y.,Mao, Y.,Yin, Y.
A conserved N-terminal motif of CUL3 contributes to assembly and E3 ligase activity of CRL3 KLHL22.
Nat Commun, 15:3789-3789, 2024

PubMed Abstract: The CUL3-RING E3 ubiquitin ligases (CRL3s) play an essential role in response to extracellular nutrition and stress stimuli. The ubiquitin ligase function of CRL3s is activated through dimerization. However, how and why such a dimeric assembly is required for its ligase activity remains elusive. Here, we report the cryo-EM structure of the dimeric CRL3 complex and reveal a conserved N-terminal motif in CUL3 that contributes to the dimerization assembly and the E3 ligase activity of CRL3. We show that deletion of the CUL3 N-terminal motif impairs dimeric assembly and the E3 ligase activity of both CRL3 and several other CRL3s. In addition, we found that the dynamics of dimeric assembly of CRL3 generates a variable ubiquitination zone, potentially facilitating substrate recognition and ubiquitination. These findings demonstrate that a CUL3 N-terminal motif participates in the assembly process and provide insights into the assembly and activation of CRL3s.

PubMed: 38710693
DOI: 10.1038/s41467-024-48045-2

Experimental method

ELECTRON MICROSCOPY (3.8 Å)