4TKP

Complex of Ubc13 with the RING domain of the TRIM5alpha retroviral restriction factor

4TKP の概要

• エントリーDOI: 10.2210/pdb4tkp/pdb
• 分子名称: Ubiquitin-conjugating enzyme E2 N, Tripartite motif-containing protein 5, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: hiv restriction, trim5, ubc13, e3 ubiquitin ligase, ring dimerization, ligase
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27773.56

構造登録者

Johnson, R.,Taylor, A.B.,Hart, P.J.,Ivanov, D.N. (登録日: 2014-05-27, 公開日: 2015-07-22, 最終更新日: 2023-12-27)

主引用文献

Yudina, Z.,Roa, A.,Johnson, R.,Biris, N.,de Souza Aranha Vieira, D.A.,Tsiperson, V.,Reszka, N.,Taylor, A.B.,Hart, P.J.,Demeler, B.,Diaz-Griffero, F.,Ivanov, D.N.
RING Dimerization Links Higher-Order Assembly of TRIM5 alpha to Synthesis of K63-Linked Polyubiquitin.
Cell Rep, 12:788-797, 2015

PubMed Abstract: Members of the tripartite motif (TRIM) protein family of RING E3 ubiquitin (Ub) ligases promote innate immune responses by catalyzing synthesis of polyubiquitin chains linked through lysine 63 (K63). Here, we investigate the mechanism by which the TRIM5α retroviral restriction factor activates Ubc13, the K63-linkage-specific E2. Structural, biochemical, and functional characterization of the TRIM5α:Ubc13-Ub interactions reveals that activation of the Ubc13-Ub conjugate requires dimerization of the TRIM5α RING domain. Our data explain how higher-order oligomerization of TRIM5α, which is promoted by the interaction with the retroviral capsid, enhances the E3 Ub ligase activity of TRIM5α and contributes to its antiretroviral function. This E3 mechanism, in which RING dimerization is transient and depends on the interaction of the TRIM protein with the ligand, is likely to be conserved in many members of the TRIM family and may have evolved to facilitate recognition of repetitive epitope patterns associated with infection.

PubMed: 26212332
DOI: 10.1016/j.celrep.2015.06.072

実験手法

X-RAY DIFFRACTION (2.08 Å)