5VZW

TRIM23 RING domain in complex with UbcH5-Ub

Summary for 5VZW

• Entry DOI: 10.2210/pdb5vzw/pdb
• Descriptor: Ubiquitin-conjugating enzyme E2 D2, Ubiquitin, E3 ubiquitin-protein ligase TRIM23, ... (5 entities in total)
• Functional Keywords: ring domain, e3 ligase, transferase-protein binding complex, transferase/protein binding
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 6
• Total formula weight: 77894.72

Authors

Pornillos, O.,Dawidziak, D. (deposition date: 2017-05-29, release date: 2017-08-09, Last modification date: 2023-10-04)

Primary citation

Dawidziak, D.M.,Sanchez, J.G.,Wagner, J.M.,Ganser-Pornillos, B.K.,Pornillos, O.
Structure and catalytic activation of the TRIM23 RING E3 ubiquitin ligase.
Proteins, 85:1957-1961, 2017

PubMed Abstract: 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.

PubMed: 28681414
DOI: 10.1002/prot.25348

Experimental method

X-RAY DIFFRACTION (2.278 Å)