6KG6

Crystal structure of MavC/UBE2N-Ub complex

6KG6 の概要

• エントリーDOI: 10.2210/pdb6kg6/pdb
• 分子名称: MavC, Ubiquitin-40S ribosomal protein S27a, Ubiquitin-conjugating enzyme E2 N, ... (4 entities in total)
• 機能のキーワード: complex, deamidase, ubiquitin, hydrolase, hydrolase-transferase complex, hydrolase/transferase
• 由来する生物種: Legionella pneumophila; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 69549.01

構造登録者

Wang, Y.,Huang, Y.,Chang, M.,Feng, Y. (登録日: 2019-07-10, 公開日: 2020-04-01, 最終更新日: 2023-11-22)

主引用文献

Mu, Y.,Wang, Y.,Huang, Y.,Li, D.,Han, Y.,Chang, M.,Fu, J.,Xie, Y.,Ren, J.,Wang, H.,Zhang, Y.,Luo, Z.Q.,Feng, Y.
Structural insights into the mechanism and inhibition of transglutaminase-induced ubiquitination by the Legionella effector MavC.
Nat Commun, 11:1774-1774, 2020

PubMed Abstract: Protein ubiquitination is one of the most prevalent post-translational modifications, controlling virtually every process in eukaryotic cells. Recently, the Legionella effector MavC was found to mediate a unique ubiquitination through transglutamination, linking ubiquitin (Ub) to UBE2N through Ub in a process that can be inhibited by another Legionella effector, Lpg2149. Here, we report the structures of MavC/UBE2N/Ub ternary complex, MavC/UBE2N-Ub (product) binary complex, and MavC/Lpg2149 binary complex. During the ubiquitination, the loop containing the modification site K92 of UBE2N undergoes marked conformational change, and Lpg2149 inhibits this ubiquitination through competing with Ub to bind MavC. Moreover, we found that MavC itself also exhibits weak deubiquitinase activity towards this non-canonical ubiquitination. Together, our study not only provides insights into the mechanism and inhibition of this transglutaminase-induced ubiquitination by MavC, but also sheds light on the future studies into UBE2N inhibition by this modification and deubiquitinases of this unique ubiquitination.

PubMed: 32286321
DOI: 10.1038/s41467-020-15645-7

実験手法

X-RAY DIFFRACTION (2.39 Å)