6AOK
Crystal structure of Legionella pneumophila effector Ceg4 with N-terminal TEV protease cleavage sequence
Summary for 6AOK
| Entry DOI | 10.2210/pdb6aok/pdb |
| Related | 6AOJ |
| Descriptor | Ceg4, MAGNESIUM ION, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | effector, legionella pneumophila, infection, had-like phosphatase, alpha/beta protein, phosphotyrosine, hydrolase |
| Biological source | Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) |
| Total number of polymer chains | 1 |
| Total formula weight | 25833.95 |
| Authors | Stogios, P.J.,Cuff, M.E.,Nocek, B.,Evdokimova, E.,Egorova, O.,Yim, V.,Di Leo, R.,Savchenko, A. (deposition date: 2017-08-16, release date: 2018-01-10, Last modification date: 2024-10-16) |
| Primary citation | Quaile, A.T.,Stogios, P.J.,Egorova, O.,Evdokimova, E.,Valleau, D.,Nocek, B.,Kompella, P.S.,Peisajovich, S.,Yakunin, A.F.,Ensminger, A.W.,Savchenko, A. TheLegionella pneumophilaeffector Ceg4 is a phosphotyrosine phosphatase that attenuates activation of eukaryotic MAPK pathways. J. Biol. Chem., 293:3307-3320, 2018 Cited by PubMed Abstract: Host colonization by Gram-negative pathogens often involves delivery of bacterial proteins called "effectors" into the host cell. The pneumonia-causing pathogen delivers more than 330 effectors into the host cell via its type IVB Dot/Icm secretion system. The collective functions of these proteins are the establishment of a replicative niche from which can recruit cellular materials to grow while evading lysosomal fusion inhibiting its growth. Using a combination of structural, biochemical, and approaches, we show that one of these translocated effector proteins, Ceg4, is a phosphotyrosine phosphatase harboring a haloacid dehalogenase-hydrolase domain. Ceg4 could dephosphorylate a broad range of phosphotyrosine-containing peptides and attenuated activation of MAPK-controlled pathways in both yeast and human cells. Our findings indicate that 's infectious program includes manipulation of phosphorylation cascades in key host pathways. The structural and functional features of the Ceg4 effector unraveled here provide first insight into its function as a phosphotyrosine phosphatase, paving the way to further studies into pathogenicity. PubMed: 29301934DOI: 10.1074/jbc.M117.812727 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.88 Å) |
Structure validation
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