6W9O

Crystal structure of an OTU deubiquitinase from Wolbachia pipientis wMel

Summary for 6W9O

• Entry DOI: 10.2210/pdb6w9o/pdb
• Descriptor: OTU domain-containing protein wMelOTU, ACETATE ION (3 entities in total)
• Functional Keywords: deubiquitinase, bacterial effector, hydrolase
• Biological source: Wolbachia pipientis wMel
• Total number of polymer chains: 1
• Total formula weight: 24547.07

Authors

Schubert, A.F.,Pruneda, J.N.,Komander, D. (deposition date: 2020-03-23, release date: 2020-07-01, Last modification date: 2023-10-18)

Primary citation

Schubert, A.F.,Nguyen, J.V.,Franklin, T.G.,Geurink, P.P.,Roberts, C.G.,Sanderson, D.J.,Miller, L.N.,Ovaa, H.,Hofmann, K.,Pruneda, J.N.,Komander, D.
Identification and characterization of diverse OTU deubiquitinases in bacteria.
Embo J., 39:e105127-e105127, 2020

PubMed Abstract: Manipulation of host ubiquitin signaling is becoming an increasingly apparent evolutionary strategy among bacterial and viral pathogens. By removing host ubiquitin signals, for example, invading pathogens can inactivate immune response pathways and evade detection. The ovarian tumor (OTU) family of deubiquitinases regulates diverse ubiquitin signals in humans. Viral pathogens have also extensively co-opted the OTU fold to subvert host signaling, but the extent to which bacteria utilize the OTU fold was unknown. We have predicted and validated a set of OTU deubiquitinases encoded by several classes of pathogenic bacteria. Biochemical assays highlight the ubiquitin and polyubiquitin linkage specificities of these bacterial deubiquitinases. By determining the ubiquitin-bound structures of two examples, we demonstrate the novel strategies that have evolved to both thread an OTU fold and recognize a ubiquitin substrate. With these new examples, we perform the first cross-kingdom structural analysis of the OTU fold that highlights commonalities among distantly related OTU deubiquitinases.

PubMed: 32567101
DOI: 10.15252/embj.2020105127

Experimental method

X-RAY DIFFRACTION (1.47 Å)