8FXF

Crystal structure of the coiled-coil domain of TRIM56

Summary for 8FXF

• Entry DOI: 10.2210/pdb8fxf/pdb
• Descriptor: E3 ubiquitin-protein ligase TRIM56, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID (2 entities in total)
• Functional Keywords: ubiquitination, coiled-coil, ligase
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 4
• Total formula weight: 40359.57

Authors

Lou, X.H.,Ma, B.B.,Zhuang, Y.,Li, X.C. (deposition date: 2023-01-24, release date: 2023-05-24, Last modification date: 2024-05-22)

Primary citation

Lou, X.,Ma, B.,Zhuang, Y.,Xiao, X.,Minze, L.J.,Xing, J.,Zhang, Z.,Li, X.C.
TRIM56 coiled-coil domain structure provides insights into its E3 ligase functions.
Comput Struct Biotechnol J, 21:2801-2808, 2023

PubMed Abstract: Protein ubiquitination is a post-translation modification mediated by E3 ubiquitin ligases. The RING domain E3 ligases are the largest family of E3 ubiquitin ligases, they act as a scaffold, bringing the E2-ubiquitin complex and its substrate together to facilitate direct ubiquitin transfer. However, the quaternary structures of RING E3 ligases that perform ubiquitin transfer remain poorly understood. In this study, we solved the crystal structure of TRIM56, a member of the RING E3 ligase. The structure of the coiled-coil domain indicated that the two anti-parallel dimers bound together to form a tetramer at a small crossing angle. This tetramer structure allows two RING domains to exist on each side to form an active homodimer in supporting ubiquitin transfer from E2 to its nearby substrate recruited by the C-terminal domains on the same side. These findings suggest that the coiled-coil domain-mediated tetramer is a feasible scaffold for facilitating the recruitment and transfer of ubiquitin to accomplish E3 ligase activity.

PubMed: 37168870
DOI: 10.1016/j.csbj.2023.04.022

Experimental method

X-RAY DIFFRACTION (2.8 Å)