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5SUJ

Crystal structure of uncharacterized protein LPG2148 from Legionella pneumophila

Summary for 5SUJ
Entry DOI10.2210/pdb5suj/pdb
DescriptorUncharacterized protein (2 entities in total)
Functional Keywordsmidwest center for structural genomics, mcsg, unknown function, psi-biology
Biological sourceLegionella pneumophila subsp. pneumophila
Total number of polymer chains2
Total formula weight92699.98
Authors
Chang, C.,Xu, X.,Cui, H.,Savchenko, A.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2016-08-03, release date: 2016-08-17, Last modification date: 2024-11-20)
Primary citationValleau, D.,Quaile, A.T.,Cui, H.,Xu, X.,Evdokimova, E.,Chang, C.,Cuff, M.E.,Urbanus, M.L.,Houliston, S.,Arrowsmith, C.H.,Ensminger, A.W.,Savchenko, A.
Discovery of Ubiquitin Deamidases in the Pathogenic Arsenal of Legionella pneumophila.
Cell Rep, 23:568-583, 2018
Cited by
PubMed Abstract: Legionella pneumophila translocates the largest known arsenal of over 330 pathogenic factors, called "effectors," into host cells during infection, enabling L. pneumophila to establish a replicative niche inside diverse amebas and human macrophages. Here, we reveal that the L. pneumophila effectors MavC (Lpg2147) and MvcA (Lpg2148) are structural homologs of cycle inhibiting factor (Cif) effectors and that the adjacent gene, lpg2149, produces a protein that directly inhibits their activity. In contrast to canonical Cifs, both MavC and MvcA contain an insertion domain and deamidate the residue Gln40 of ubiquitin but not Gln40 of NEDD8. MavC and MvcA are functionally diverse, with only MavC interacting with the human E2-conjugating enzyme UBE2N (Ubc13). MavC deamidates the UBE2N∼Ub conjugate, disrupting Lys63 ubiquitination and dampening NF-κB signaling. Combined, our data reveal a molecular mechanism of host manipulation by pathogenic bacteria and highlight the complex regulatory mechanisms integral to L. pneumophila's pathogenic strategy.
PubMed: 29642013
DOI: 10.1016/j.celrep.2018.03.060
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.356 Å)
Structure validation

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