7bu0 | pdb_00007bu0

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

spinqualitylabelsall models 7bu0, resolution 2.43Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7bu0 is a 4 chain structure with sequence from Homo sapiens and Legionella pneumophila subsp. pneumophila str. Philadelphia 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AYE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5ZSI8_LEGPH Publication Abstract from PubMed Legionella pneumophila 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 L. pneumophila phagosomes by counteracting the activity of bacterial ubiquitin E3 ligases. Interplay between bacterial deubiquitinase and ubiquitin E3 ligase regulates ubiquitin dynamics on Legionella phagosomes.,Liu S, Luo J, Zhen X, Qiu J, Ouyang S, Luo ZQ Elife. 2020 Nov 2;9:e58114. doi: 10.7554/eLife.58114. PMID:33136002 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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