5FEY

TRIM32 RING

Summary for 5FEY

• Entry DOI: 10.2210/pdb5fey/pdb
• Descriptor: E3 ubiquitin-protein ligase TRIM32, ZINC ION (3 entities in total)
• Functional Keywords: e3 ligase, ubiquitin, ligase
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm: Q13049
• Total number of polymer chains: 2
• Total formula weight: 21660.61

Authors

Rittinger, K.,Esposito, D.,Koliopoulos, M.G. (deposition date: 2015-12-17, release date: 2016-05-18, Last modification date: 2024-05-08)

Primary citation

Koliopoulos, M.G.,Esposito, D.,Christodoulou, E.,Taylor, I.A.,Rittinger, K.
Functional role of TRIM E3 ligase oligomerization and regulation of catalytic activity.
Embo J., 35:1204-1218, 2016

PubMed Abstract: TRIM E3 ubiquitin ligases regulate a wide variety of cellular processes and are particularly important during innate immune signalling events. They are characterized by a conserved tripartite motif in their N-terminal portion which comprises a canonical RING domain, one or two B-box domains and a coiled-coil region that mediates ligase dimerization. Self-association via the coiled-coil has been suggested to be crucial for catalytic activity of TRIMs; however, the precise molecular mechanism underlying this observation remains elusive. Here, we provide a detailed characterization of the TRIM ligases TRIM25 and TRIM32 and show how their oligomeric state is linked to catalytic activity. The crystal structure of a complex between the TRIM25 RING domain and an ubiquitin-loaded E2 identifies the structural and mechanistic features that promote a closed E2~Ub conformation to activate the thioester for ubiquitin transfer allowing us to propose a model for the regulation of activity in the full-length protein. Our data reveal an unexpected diversity in the self-association mechanism of TRIMs that might be crucial for their biological function.

PubMed: 27154206
DOI: 10.15252/embj.201593741

Experimental method

X-RAY DIFFRACTION (2.23 Å)