6CGK
Structure of the HAD domain of effector protein Lem4 (lpg1101) from Legionella pneumophila (inactive mutant)with phosphate bound in the active site
Summary for 6CGK
| Entry DOI | 10.2210/pdb6cgk/pdb |
| Related | 6CDW 6CGJ |
| Descriptor | effector protein Lem4 (lpg1101), PHOSPHATE ION, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | haloacid dehalogenase superfamily, tyrosine phosphatase, translocated bacterial effector, hydrolase |
| Biological source | Legionella pneumophila subsp. pneumophila |
| Total number of polymer chains | 1 |
| Total formula weight | 24916.20 |
| Authors | Beyrakhova, K.A.,Xu, C.,Cygler, M. (deposition date: 2018-02-20, release date: 2018-07-18, Last modification date: 2023-10-04) |
| Primary citation | Beyrakhova, K.,Li, L.,Xu, C.,Gagarinova, A.,Cygler, M. Legionella pneumophilaeffector Lem4 is a membrane-associated protein tyrosine phosphatase. J. Biol. Chem., 293:13044-13058, 2018 Cited by PubMed Abstract: is a Gram-negative pathogenic bacterium that causes severe pneumonia in humans. It establishes a replicative niche called -containing vacuole (LCV) that allows bacteria to survive and replicate inside pulmonary macrophages. To hijack host cell defense systems, injects over 300 effector proteins into the host cell cytosol. The Lem4 effector (lpg1101) consists of two domains: an N-terminal haloacid dehalogenase (HAD) domain with unknown function and a C-terminal phosphatidylinositol 4-phosphate-binding domain that anchors Lem4 to the membrane of early LCVs. Herein, we demonstrate that the HAD domain (Lem4-N) is structurally similar to mouse MDP-1 phosphatase and displays phosphotyrosine phosphatase activity. Substrate specificity of Lem4 was probed using a tyrosine phosphatase substrate set, which contained a selection of 360 phosphopeptides derived from human phosphorylation sites. This assay allowed us to identify a consensus pTyr-containing motif. Based on the localization of Lem4 to lysosomes and to some extent to plasma membrane when expressed in human cells, we hypothesize that this protein is involved in protein-protein interactions with an LCV or plasma membrane-associated tyrosine-phosphorylated host target. PubMed: 29976756DOI: 10.1074/jbc.RA118.003845 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.668 Å) |
Structure validation
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