8bvp

Crystal structure of an N-terminal fragment of the effector protein Lpg2504 (SidI) from Legionella pneumophila

spinqualitylabelsall models 8bvp, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8bvp is a 1 chain structure with sequence from Legionella pneumophila. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: CL, EDO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5ZSL3_LEGPH Publication Abstract from PubMed The Gram-negative bacterium Legionella pneumophila is an accidental human pathogen that can cause a life-threatening respiratory infection called Legionellosis. In the course of infection, L. pneumophila injects more than 300 effector proteins into the host cell. The effector proteins modify the intracellular environment in order to create a stable compartment for proliferation within the host cell. The effector protein SidI has been shown to potently inhibit host translation upon translocation. SidI is able to interact with the translation elongation factor eEF1A, which has been hypothesized to be a target of SidI. A postulated glycosyltransferase domain in the C-terminal half may be responsible for the toxic effect of SidI. Here, we present the crystal structure of an N-terminal fragment of SidI containing residues 37-573. The structure is divided into three subdomains, two of which display a novel fold. The third subdomain shows close structural homology to GT-B fold glycosyltransferases. Based on structural analysis we predict that the two previously identified residues R453 and E482 assume roles in the catalytic activity of SidI. Furthermore, we show that the N-terminal fragment of SidI is able to directly interact with a postulated target, the translation elongation factor eEF1A. Crystal structure of the N-terminal domain of the effector protein SidI of Legionella pneumophila reveals a glucosyl transferase domain.,Machtens DA, Willerding JM, Eschenburg S, Reubold TF Biochem Biophys Res Commun. 2023 Jun 18;661:50-55. doi: , 10.1016/j.bbrc.2023.04.029. Epub 2023 Apr 14. PMID:37087798 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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