6YK8

OTU-like deubiquitinase from Legionella -Lpg2529

Summary for 6YK8

• Entry DOI: 10.2210/pdb6yk8/pdb
• Descriptor: Uncharacterized protein, PLATINUM (II) ION (3 entities in total)
• Functional Keywords: deubiquitinase, legionella, otu, effector protein, cell invasion
• Biological source: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
• Total number of polymer chains: 2
• Total formula weight: 71454.94

Authors

Shin, D.,Dikic, I. (deposition date: 2020-04-05, release date: 2021-02-10, Last modification date: 2024-05-15)

Primary citation

Shin, D.,Bhattacharya, A.,Cheng, Y.L.,Alonso, M.C.,Mehdipour, A.R.,van der Heden van Noort, G.J.,Ovaa, H.,Hummer, G.,Dikic, I.
Bacterial OTU deubiquitinases regulate substrate ubiquitination upon Legionella infection.
Elife, 9:-, 2020

PubMed Abstract: causes a severe pneumonia known as Legionnaires' disease. During the infection, Legionella injects more than 300 effector proteins into host cells. Among them are enzymes involved in altering the host-ubiquitination system. Here, we identified two egionellaU (ovarian tumor)-like deubiquitinases (LOT-DUBs; LotB [Lpg1621/Ceg23] and LotC [Lpg2529]). The crystal structure of the LotC catalytic core (LotC) was determined at 2.4 Å. Unlike the classical OTU-family, the LOT-family shows an extended helical lobe between the Cys-loop and the variable loop, which defines them as a unique class of OTU-DUBs. LotB has an additional ubiquitin-binding site (S1'), which enables the specific cleavage of Lys63-linked polyubiquitin chains. By contrast, LotC only contains the S1 site and cleaves different species of ubiquitin chains. MS analysis of LotB and LotC identified different categories of host-interacting proteins and substrates. Together, our results provide new structural insights into bacterial OTU-DUBs and indicate distinct roles in host-pathogen interactions.

PubMed: 33185526
DOI: 10.7554/eLife.58277

Experimental method

X-RAY DIFFRACTION (2.42 Å)