7Y3B

Crystal structure of TRIM7 bound to GN1

Summary for 7Y3B

• Entry DOI: 10.2210/pdb7y3b/pdb
• Descriptor: E3 ubiquitin-protein ligase TRIM7,TRIM7-GN1 (2 entities in total)
• Functional Keywords: e3 ligase, cytosolic protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 1
• Total formula weight: 21196.88

Authors

Dong, C.,Yan, X. (deposition date: 2022-06-10, release date: 2022-08-03, Last modification date: 2023-11-29)

Primary citation

Ru, Y.,Yan, X.,Zhang, B.,Song, L.,Feng, Q.,Ye, C.,Zhou, Z.,Yang, Z.,Li, Y.,Zhang, Z.,Li, Q.,Mi, W.,Dong, C.
C-terminal glutamine acts as a C-degron targeted by E3 ubiquitin ligase TRIM7.
Proc.Natl.Acad.Sci.USA, 119:e2203218119-e2203218119, 2022

PubMed Abstract: The exposed N-terminal or C-terminal residues of proteins can act, in cognate sequence contexts, as degradation signals (degrons) that are targeted by specific E3 ubiquitin ligases for proteasome-dependent degradation by -degron or C-degron pathways. Here, we discovered a distinct C-degron pathway, termed the Gln/C-degron pathway, in which the B30.2 domain of E3 ubiquitin ligase TRIM7 (TRIM7) mediates the recognition of proteins bearing a C-terminal glutamine. By determining crystal structures of TRIM7 in complexes with various peptides, we show that TRIM7 forms a positively charged binding pocket to engage the "U"-shaped Gln/C-degron. The four C-terminal residues of a substrate play an important role in C-degron recognition, with C-terminal glutamine as the principal determinant. In vitro biochemical and cellular experiments were used to further analyze the substrate specificity and selective degradation of the Gln/C-degron by TRIM7.

PubMed: 35867826
DOI: 10.1073/pnas.2203218119

Experimental method

X-RAY DIFFRACTION (1.76 Å)