Structure of a TRAF6-Ubc13~Ub complexStructure of a TRAF6-Ubc13~Ub complex

Structural highlights

5vo0 is a 6 chain structure with sequence from Danio rerio and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.9Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TRAF6_DANRE E3 ubiquitin-protein ligase that mediates ubiquitination of proteins. Adapter protein that seems to play a role in signal transduction.

Publication Abstract from PubMed

Ubiquitin chains linked through lysine63 (K63) play a critical role in inflammatory signalling. Following ligand engagement of immune receptors, the RING E3 ligase TRAF6 builds K63-linked chains together with the heterodimeric E2 enzyme Ubc13-Uev1A. Dimerisation of the TRAF6 RING domain is essential for the assembly of K63-linked ubiquitin chains. Here, we show that TRAF6 RING dimers form a catalytic complex where one RING interacts with a Ubc13~Ubiquitin conjugate, while the zinc finger 1 (ZF1) domain and linker-helix of the opposing monomer contact ubiquitin. The RING dimer interface is conserved across TRAFs and we also show that TRAF5-TRAF6 heterodimers form. Importantly, TRAF5 can provide ZF1, enabling ubiquitin transfer from a TRAF6-bound Ubc13 conjugate. Our study explains the dependence of activity on TRAF RING dimers, and suggests that both homo- and heterodimers mediated by TRAF RING domains have the capacity to synthesise ubiquitin chains.

The activity of TRAF RING homo- and heterodimers is regulated by zinc finger 1.,Middleton AJ, Budhidarmo R, Das A, Zhu J, Foglizzo M, Mace PD, Day CL Nat Commun. 2017 Nov 27;8(1):1788. doi: 10.1038/s41467-017-01665-3. PMID:29176576[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Middleton AJ, Budhidarmo R, Das A, Zhu J, Foglizzo M, Mace PD, Day CL. The activity of TRAF RING homo- and heterodimers is regulated by zinc finger 1. Nat Commun. 2017 Nov 27;8(1):1788. doi: 10.1038/s41467-017-01665-3. PMID:29176576 doi:http://dx.doi.org/10.1038/s41467-017-01665-3

5vo0, resolution 3.90Å

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