Structure and catalytic activation of the TRIM23 RING E3 ubiquitin ligase: DAWIDZIAK et al.

Dawidziak, Daria M.; Sanchez, Jacint G.; Wagner, Jonathan M.; Ganser-Pornillos, Barbie K.; Pornillos, Owen

doi:10.1002/prot.25348

Structure and catalytic activation of the TRIM23 RING E3 ubiquitin ligase: DAWIDZIAK et al.

Journal Article · Mon Jul 24 00:00:00 EDT 2017 · Proteins

DOI:https://doi.org/10.1002/prot.25348· OSTI ID:1397295

Dawidziak, Daria M. ^[1]; Sanchez, Jacint G. ^[1]; Wagner, Jonathan M. ^[1]; Ganser-Pornillos, Barbie K. ^[1]; ^[1]

Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville Virginia

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.

Research Organization:: Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)

Sponsoring Organization:: NIH

OSTI ID:: 1397295

Journal Information:: Proteins, Journal Name: Proteins Journal Issue: 10 Vol. 85; ISSN 0887-3585

Publisher:: Wiley

Country of Publication:: United States

Language:: ENGLISH

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