8OI3

Structure of NopD with AtSUMO2

8OI3 の概要

• エントリーDOI: 10.2210/pdb8oi3/pdb
• 分子名称: Type III effector, Small ubiquitin-related modifier 2, prop-2-en-1-amine, ... (4 entities in total)
• 機能のキーワード: sumo protease, complex, plant sumo2, hydrolase
• 由来する生物種: Bradyrhizobium; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 67973.81

構造登録者

Reverter, D.,Li, Y. (登録日: 2023-03-22, 公開日: 2024-04-03, 最終更新日: 2026-03-04)

主引用文献

Li, Y.,Perez-Gil, J.,Lois, L.M.,Varejao, N.,Reverter, D.
Broad-spectrum ubiquitin/ubiquitin-like deconjugation activity of the rhizobial effector NopD from Bradyrhizobium (sp. XS1150).
Commun Biol, 7:644-644, 2024

PubMed Abstract: The post-translational modification of proteins by ubiquitin-like modifiers (UbLs), such as SUMO, ubiquitin, and Nedd8, regulates a vast array of cellular processes. Dedicated UbL deconjugating proteases families reverse these modifications. During bacterial infection, effector proteins, including deconjugating proteases, are released to disrupt host cell defenses and promote bacterial survival. NopD, an effector protein from rhizobia involved in legume nodule symbiosis, exhibits deSUMOylation activity and, unexpectedly, also deubiquitination and deNeddylation activities. Here, we present two crystal structures of Bradyrhizobium (sp. XS1150) NopD complexed with either Arabidopsis SUMO2 or ubiquitin at 1.50 Å and 1.94 Å resolution, respectively. Despite their low sequence similarity, SUMO and ubiquitin bind to a similar NopD interface, employing a unique loop insertion in the NopD sequence. In vitro binding and activity assays reveal specific residues that distinguish between deubiquitination and deSUMOylation. These unique multifaceted deconjugating activities against SUMO, ubiquitin, and Nedd8 exemplify an optimized bacterial protease that disrupts distinct UbL post-translational modifications during host cell infection.

PubMed: 38802699
DOI: 10.1038/s42003-024-06344-w

実験手法

X-RAY DIFFRACTION (1.5 Å)