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6KS5

Crystal structure of Legionella pneumophila deubiquitinase Ceg23

Summary for 6KS5
Entry DOI10.2210/pdb6ks5/pdb
DescriptorType IV secretion protein Dot (1 entity in total)
Functional Keywordsenzyme, hydrolase
Biological sourceLegionella pneumophila
Total number of polymer chains2
Total formula weight81597.47
Authors
Qiu, J.Z.,Ouyang, S.Y. (deposition date: 2019-08-23, release date: 2020-01-15, Last modification date: 2024-03-27)
Primary citationMa, K.,Zhen, X.,Zhou, B.,Gan, N.,Cao, Y.,Fan, C.,Ouyang, S.,Luo, Z.Q.,Qiu, J.
The bacterial deubiquitinase Ceg23 regulates the association of Lys-63-linked polyubiquitin molecules on theLegionellaphagosome.
J.Biol.Chem., 295:1646-1657, 2020
Cited by
PubMed Abstract: is the causative agent of the lung malady Legionnaires' disease, it modulates host function to create a niche termed the -containing vacuole (LCV) that permits intracellular replication. One important aspect of such modulation is the co-option of the host ubiquitin network with a panel of effector proteins. Here, using recombinantly expressed and purified proteins, analytic ultracentrifugation, structural analysis, and computational modeling, along with deubiquitinase (DUB), and bacterial infection assays, we found that the bacterial defective in organelle trafficking/intracellular multiplication effector Ceg23 is a member of the ovarian tumor (OTU) DUB family. We found that Ceg23 displays high specificity toward Lys-63-linked polyubiquitin chains and is localized on the LCV, where it removes ubiquitin moieties from proteins ubiquitinated by the Lys-63-chain type. Analysis of the crystal structure of a Ceg23 variant lacking two putative transmembrane domains at 2.80 Å resolution revealed that despite very limited homology to established members of the OTU family at the primary sequence level, Ceg23 harbors a catalytic motif resembling those associated with typical OTU-type DUBs. deletion increased the association of Lys-63-linked polyubiquitin with the bacterial phagosome, indicating that Ceg23 regulates Lys-63-linked ubiquitin signaling on the LCV. In summary, our findings indicate that Ceg23 contributes to the regulation of the association of Lys-63 type polyubiquitin with the phagosome. Future identification of host substrates targeted by Ceg23 could clarify the roles of these polyubiquitin chains in the intracellular life cycle of and Ceg23's role in bacterial virulence.
PubMed: 31907282
DOI: 10.1074/jbc.RA119.011758
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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數據於2025-07-30公開中

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