8PZ3

TssM - A USP-like DUB from B. pseudomallei (193-430)

8PZ3 の概要

• エントリーDOI: 10.2210/pdb8pz3/pdb
• 分子名称: TssM (1 entity in total)
• 機能のキーワード: deubiquitinase, papain-fold, usp, hydrolase
• 由来する生物種: Burkholderia pseudomallei
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64314.03

構造登録者

Uthoff, M.,Hermanns, T.,Hofmann, K.,Baumann, U. (登録日: 2023-07-26, 公開日: 2023-12-13, 最終更新日: 2024-01-17)

主引用文献

Hermanns, T.,Uthoff, M.,Baumann, U.,Hofmann, K.
The structural basis for deubiquitination by the fingerless USP-type effector TssM.
Life Sci Alliance, 7:-, 2024

PubMed Abstract: Intracellular bacteria are threatened by ubiquitin-mediated autophagy, whenever the bacterial surface or enclosing membrane structures become targets of host ubiquitin ligases. As a countermeasure, many intracellular pathogens encode deubiquitinase (DUB) effectors to keep their surfaces free of ubiquitin. Most bacterial DUBs belong to the OTU or CE-clan families. The betaproteobacteria and , causative agents of melioidosis and glanders, respectively, encode the TssM effector, the only known bacterial DUB belonging to the USP class. TssM is much shorter than typical eukaryotic USP enzymes and lacks the canonical ubiquitin-recognition region. By solving the crystal structures of isolated TssM and its complex with ubiquitin, we found that TssM lacks the entire "Fingers" subdomain of the USP fold. Instead, the TssM family has evolved the functionally analog "Littlefinger" loop, which is located towards the end of the USP domain and recognizes different ubiquitin interfaces than those used by USPs. The structures revealed the presence of an N-terminal immunoglobulin-fold domain, which is able to form a strand-exchange dimer and might mediate TssM localization to the bacterial surface.

PubMed: 38170641
DOI: 10.26508/lsa.202302422

実験手法

X-RAY DIFFRACTION (3.15 Å)