3SY2

Crystal structure of the Salmonella E3 ubiquitin ligase SopA in complex with the human E2 UbcH7

3SY2 の概要

• エントリーDOI: 10.2210/pdb3sy2/pdb
• 分子名称: E3 ubiquitin-protein ligase SopA, Ubiquitin-conjugating enzyme E2 L3, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: pentapeptide, hect domain, hect e3, hect e3 ubiquitin ligase, e2 ubiquitin conjugating enzyme, ubiquitin, protein-protein complex, effector protein, ubiquitin transfer, ubiquitination, ligase-signaling protein complex, ligase/signaling protein
• 由来する生物種: Salmonella enterica subsp. enterica serovar Typhimurium; 詳細
• 細胞内の位置: Secreted: Q8ZNR3; Nucleus: P68036
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 174633.95

構造登録者

Diao, J.,Lin, D.Y.,Chen, J. (登録日: 2011-07-15, 公開日: 2012-01-25, 最終更新日: 2023-09-13)

主引用文献

Lin, D.Y.,Diao, J.,Chen, J.
Crystal structures of two bacterial HECT-like E3 ligases in complex with a human E2 reveal atomic details of pathogen-host interactions.
Proc.Natl.Acad.Sci.USA, 109:1925-1930, 2012

PubMed Abstract: In eukaryotes, ubiquitination is an important posttranslational process achieved through a cascade of ubiquitin-activating (E1), conjugating (E2), and ligase (E3) enzymes. Many pathogenic bacteria deliver virulence factors into the host cell that function as E3 ligases. How these bacterial "Trojan horses" integrate into the eukaryotic ubiquitin system has remained a mystery. Here we report crystal structures of two bacterial E3s, Salmonella SopA and Escherichia coli NleL, both in complex with human E2 UbcH7. These structures represent two distinct conformational states of the bacterial E3s, supporting the necessary structural rearrangements associated with ubiquitin transfer. The E2-interacting surface of SopA and NleL has little similarity to those of eukaryotic E3s. However, both bacterial E3s bind to the canonical surface of E2 that normally interacts with eukaryotic E3s. Furthermore, we show that a glutamate residue on E3 is involved in catalyzing ubiquitin transfer from E3 to the substrate, but not from E2 to E3. Together, these results provide mechanistic insights into the ubiquitin pathway and a framework for understanding molecular mimicry in bacterial pathogenesis.

PubMed: 22308380
DOI: 10.1073/pnas.1115025109

実験手法

X-RAY DIFFRACTION (3.27 Å)