6YXE

Structure of the Trim69 RING domain

Summary for 6YXE

• Entry DOI: 10.2210/pdb6yxe/pdb
• Descriptor: E3 ubiquitin-protein ligase TRIM69, ZINC ION (3 entities in total)
• Functional Keywords: trim69, tripartite motif, trim protein, antiviral protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 29743.65

Authors

Keown, J.R.,Goldstone, D.C. (deposition date: 2020-05-01, release date: 2020-10-14, Last modification date: 2024-05-15)

Primary citation

Keown, J.R.,Yang, J.,Black, M.M.,Goldstone, D.C.
The RING domain of TRIM69 promotes higher-order assembly.
Acta Crystallogr D Struct Biol, 76:954-961, 2020

PubMed Abstract: Members of the TRIM protein family have been shown to inhibit a range of viral infections. Recently, TRIM69 was identified as a potent inhibitor of Vesicular stomatitis Indiana virus infection, with its inhibition being dependent upon multimerization. Using SEC-MALLS analysis, it is demonstrated that the assembly of TRIM69 is mediated through the RING domain and not the Bbox domain as has been shown for other TRIM proteins. Using X-ray crystallography, the structure of the TRIM69 RING domain has been determined to a resolution of 2.1 Å, the oligomerization interface has been identified and regions outside the four-helix bundle have been observed to form interactions that are likely to support assembly.

PubMed: 33021497
DOI: 10.1107/S2059798320010499

Experimental method

X-RAY DIFFRACTION (2.1 Å)