8PZ3

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

Summary for 8PZ3

• Entry DOI: 10.2210/pdb8pz3/pdb
• Descriptor: TssM (1 entity in total)
• Functional Keywords: deubiquitinase, papain-fold, usp, hydrolase
• Biological source: Burkholderia pseudomallei
• Total number of polymer chains: 2
• Total formula weight: 64314.03

Authors

Uthoff, M.,Hermanns, T.,Hofmann, K.,Baumann, U. (deposition date: 2023-07-26, release date: 2023-12-13, Last modification date: 2024-01-17)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.15 Å)