5JW7

Crystal structure of SopA-Trim56 complex

5JW7 の概要

• エントリーDOI: 10.2210/pdb5jw7/pdb
• 分子名称: E3 ubiquitin-protein ligase SopA, E3 ubiquitin-protein ligase TRIM56, ZINC ION, ... (4 entities in total)
• 機能のキーワード: ubiquitination, bacterial effector, sopa, trim56, ligase
• 由来する生物種: Salmonella enterica subsp. enterica serovar Typhimurium; 詳細
• 細胞内の位置: Secreted : Q8ZNR3; Cytoplasm : Q9BRZ2
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41371.23

構造登録者

Bhogaraju, S.,Dikic, I. (登録日: 2016-05-11, 公開日: 2017-02-15, 最終更新日: 2024-01-10)

主引用文献

Fiskin, E.,Bhogaraju, S.,Herhaus, L.,Kalayil, S.,Hahn, M.,Dikic, I.
Structural basis for the recognition and degradation of host TRIM proteins by Salmonella effector SopA.
Nat Commun, 8:14004-14004, 2017

PubMed Abstract: The hallmark of Salmonella Typhimurium infection is an acute intestinal inflammatory response, which is mediated through the action of secreted bacterial effector proteins. The pro-inflammatory Salmonella effector SopA is a HECT-like E3 ligase, which was previously proposed to activate host RING ligases TRIM56 and TRIM65. Here we elucidate an inhibitory mechanism of TRIM56 and TRIM65 targeting by SopA. We present the crystal structure of SopA in complex with the RING domain of human TRIM56, revealing the atomic details of their interaction and the basis for SopA selectivity towards TRIM56 and TRIM65. Structure-guided biochemical analysis shows that SopA inhibits TRIM56 E3 ligase activity by occluding the E2-interacting surface of TRIM56. We further demonstrate that SopA ubiquitinates TRIM56 and TRIM65, resulting in their proteasomal degradation during infection. Our results provide the basis for how a bacterial HECT ligase blocks host RING ligases and exemplifies the multivalent power of bacterial effectors during infection.

PubMed: 28084320
DOI: 10.1038/ncomms14004

実験手法

X-RAY DIFFRACTION (2.849 Å)