2QYU

Crystal structure of Salmonella effector protein SopA

2QYU の概要

• エントリーDOI: 10.2210/pdb2qyu/pdb
• 関連するPDBエントリー: 2QZA
• 分子名称: Secreted effector protein, PHOSPHATE ION, 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• 機能のキーワード: ubiquitin e3 ligase, ligase
• 由来する生物種: Salmonella typhimurium
• 細胞内の位置: Secreted: Q8ZNR3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 70472.53

構造登録者

Diao, J.,Chen, J. (登録日: 2007-08-15, 公開日: 2007-12-11, 最終更新日: 2024-04-03)

主引用文献

Diao, J.,Zhang, Y.,Huibregtse, J.M.,Zhou, D.,Chen, J.
Crystal structure of SopA, a Salmonella effector protein mimicking a eukaryotic ubiquitin ligase.
Nat.Struct.Mol.Biol., 15:65-70, 2008

PubMed Abstract: Bacterial pathogens deliver virulence proteins into host cells to facilitate entry and survival. Salmonella SopA functions as an E3 ligase to manipulate the host proinflammatory response. Here we report the crystal structure of SopA in two conformations. Although it has little sequence similarity to eukaryotic HECT-domain E3s, the C-terminal half of SopA has a bilobal architecture that is reminiscent of the N- and C-lobe arrangement of HECT domains. The SopA structure also contains a putative substrate-binding domain located near the E2-binding site. The two structures of SopA differ in the relative orientations of the C lobe, indicating that SopA possesses the conformational flexibility essential for HECT E3 function. These results suggest that SopA is a unique HECT E3 ligase evolved from the coevolutionary selective pressure at the bacterium-host interface.

PubMed: 18066077
DOI: 10.1038/nsmb1346

実験手法

X-RAY DIFFRACTION (2.1 Å)