7BU0

Crystal structure of a OTU deubiquitinase in complex with Ub-PA

Summary for 7BU0

• Entry DOI: 10.2210/pdb7bu0/pdb
• Descriptor: Uncharacterized protein, Polyubiquitin-B, prop-2-en-1-amine, ... (4 entities in total)
• Functional Keywords: complex, hydrolase
• Biological source: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513); More
• Total number of polymer chains: 4
• Total formula weight: 114576.60

Authors

Ouyang, S.Y.,Zhen, X.K. (deposition date: 2020-04-03, release date: 2020-11-18, Last modification date: 2023-04-05)

Primary citation

Liu, S.,Jiwei, L.,Zhen, X.,Qiu, J.,Ouyang, S.,Luo, Z.Q.
Interplay between bacterial deubiquitinase and ubiquitin E3 ligase regulates ubiquitin dynamics on Legionella phagosomes.
Elife, 9:-, 2020

PubMed Abstract: extensively modulates the host ubiquitin network to create the Legionella-containing vacuole (LCV) for its replication. Many of its virulence factors function as ubiquitin ligases or deubiquitinases (DUBs). Here, we identify Lem27 as a DUB that displays a preference for diubiquitin formed by K6, K11, or K48. Lem27 is associated with the LCV where it regulates Rab10 ubiquitination in concert with SidC and SdcA, two bacterial E3 ubiquitin ligases. Structural analysis of the complex formed by an active fragment of Lem27 and the substrate-based suicide inhibitor ubiquitin-propargylamide (PA) reveals that it harbors a fold resembling those in the OTU1 DUB subfamily with a Cys-His catalytic dyad and that it recognizes ubiquitin via extensive hydrogen bonding at six contact sites. Our results establish Lem27 as a DUB that functions to regulate protein ubiquitination on phagosomes by counteracting the activity of bacterial ubiquitin E3 ligases.

PubMed: 33136002
DOI: 10.7554/eLife.58114

Experimental method

X-RAY DIFFRACTION (2.43 Å)