Structure and catalytic activation of the TRIM23 RING E3 ubiquitin ligase.

Tripartite motif (TRIM) proteins comprise a large family of RING-type ubiquitin E3 ligases that regulate important biological processes. An emerging general model is that TRIMs form elongated antiparallel coiled-coil dimers that prevent interaction of the two attendant RING domains. The RING domains themselves bind E2 conjugating enzymes as dimers, implying ...
that an active TRIM ligase requires higher-order oligomerization of the basal coiled-coil dimers. Here, we report crystal structures of the TRIM23 RING domain in isolation and in complex with an E2-ubiquitin conjugate. Our results indicate that TRIM23 enzymatic activity requires RING dimerization, consistent with the general model of TRIM activation.
Mesh Terms:
Crystallography, X-Ray, Dimerization, GTP-Binding Proteins, Humans, Protein Conformation, Structure-Activity Relationship, Tripartite Motif Proteins, Ubiquitin-Protein Ligases, Ubiquitination
Proteins
Date: Oct. 01, 2017
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