5JG4
Structure of the effector protein LpiR1 (Lpg0634) from Legionella pneumophila
Summary for 5JG4
Entry DOI | 10.2210/pdb5jg4/pdb |
Related | 5FIA |
Descriptor | effector protein LpiR1, PHOSPHATE ION, CITRATE ANION, ... (5 entities in total) |
Functional Keywords | legionella pneumophila, bacterial effector, phosphate binding, signaling protein |
Biological source | Legionella pneumophila |
Total number of polymer chains | 2 |
Total formula weight | 101930.65 |
Authors | Beyrakhova, K.,van Straaten, K.,Cygler, M. (deposition date: 2016-04-19, release date: 2016-05-04, Last modification date: 2024-03-06) |
Primary citation | Beyrakhova, K.A.,van Straaten, K.,Li, L.,Boniecki, M.T.,Anderson, D.H.,Cygler, M. Structural and Functional Investigations of the Effector Protein LpiR1 from Legionella pneumophila. J.Biol.Chem., 291:15767-15777, 2016 Cited by PubMed Abstract: Legionella pneumophila is a causative agent of a severe pneumonia, known as Legionnaires' disease. Legionella pathogenicity is mediated by specific virulence factors, called bacterial effectors, which are injected into the invaded host cell by the bacterial type IV secretion system. Bacterial effectors are involved in complex interactions with the components of the host cell immune and signaling pathways, which eventually lead to bacterial survival and replication inside the mammalian cell. Structural and functional studies of bacterial effectors are, therefore, crucial for elucidating the mechanisms of Legionella virulence. Here we describe the crystal structure of the LpiR1 (Lpg0634) effector protein and investigate the effects of its overexpression in mammalian cells. LpiR1 is an α-helical protein that consists of two similar domains aligned in an antiparallel fashion. The hydrophilic cleft between the domains might serve as a binding site for a potential host cell interaction partner. LpiR1 binds the phosphate group at a conserved site and is stabilized by Mn(2+), Ca(2+), or Mg(2+) ions. When overexpressed in mammalian cells, a GFP-LpiR1 fusion protein is localized in the cytoplasm. Intracellular signaling antibody array analysis revealed small changes in the phosphorylation state of several components of the Akt signaling pathway in HEK293T cells overexpressing LpiR1. PubMed: 27226543DOI: 10.1074/jbc.M115.708701 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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