7X70

TRIM7 in complex with C-terminal peptide of NSP8

Summary for 7X70

• Entry DOI: 10.2210/pdb7x70/pdb
• Descriptor: E3 ubiquitin-protein ligase TRIM7, peptide (3 entities in total)
• Functional Keywords: antiviral protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 20247.98

Authors

Zhang, H.,Liang, X.,Li, X.Z. (deposition date: 2022-03-08, release date: 2022-08-10, Last modification date: 2023-11-29)

Primary citation

Liang, X.,Xiao, J.,Li, X.,Liu, Y.,Lu, Y.,Wen, Y.,Li, Z.,Che, X.,Ma, Y.,Zhang, X.,Zhang, Y.,Jian, D.,Wang, P.,Xuan, C.,Yu, G.,Li, L.,Zhang, H.
A C-terminal glutamine recognition mechanism revealed by E3 ligase TRIM7 structures.
Nat.Chem.Biol., 18:1214-1223, 2022

PubMed Abstract: The E3 ligase TRIM7 has emerged as a critical player in viral infection and pathogenesis. However, the mechanism governing the TRIM7-substrate association remains to be defined. Here we report the crystal structures of TRIM7 in complex with 2C peptides of human enterovirus. Structure-guided studies reveal the C-terminal glutamine residue of 2C as the primary determinant for TRIM7 binding. Leveraged by this finding, we identify norovirus and SARS-CoV-2 proteins, and physiological proteins, as new TRIM7 substrates. Crystal structures of TRIM7 in complex with multiple peptides derived from SARS-CoV-2 proteins display the same glutamine-end recognition mode. Furthermore, TRIM7 could trigger the ubiquitination and degradation of these substrates, possibly representing a new Gln/C-degron pathway. Together, these findings unveil a common recognition mode by TRIM7, providing the foundation for further mechanistic characterization of antiviral and cellular functions of TRIM7.

PubMed: 35982226
DOI: 10.1038/s41589-022-01128-x

Experimental method

X-RAY DIFFRACTION (1.25 Å)