5VZV

TRIM23 RING domain

Summary for 5VZV

Entry DOI	10.2210/pdb5vzv/pdb
Descriptor	E3 ubiquitin-protein ligase TRIM23, ZINC ION (3 entities in total)
Functional Keywords	ring domain, e3 ligase, transferase
Biological source	Homo sapiens (Human)
Total number of polymer chains	3
Total formula weight	39710.62
Authors	Pornillos, O.,Dawidziak, D. (deposition date: 2017-05-29, release date: 2017-08-09, Last modification date: 2024-04-03)
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 Cited by 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 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.812 Å)

Structure validation