6deh | pdb_00006deh

Structure of LpnE Effector Protein from Legionella pneumophila (sp. Philadelphia)

spinqualitylabelsall models 6deh, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6deh is a 2 chain structure with sequence from Legionella pneumophila subsp. pneumophila str. Philadelphia 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: GOL, NI, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5ZTE0_LEGPH Publication Abstract from PubMed Legionella pneumophila is a freshwater bacterium that replicates in predatory amoeba and alveolar macrophage. The ability of L. pneumophila to thrive in eukaryotic host cells is conferred by the Legionella containing vacuole (LCV). Formation and intracellular trafficking of the LCV is governed by an arsenal of effector proteins, many of which are secreted by the Icm/Dot Type 4 Secretion System. One such effector, known as LpnE (L. pneumophila Entry), has been implicated in facilitating bacterial entry into host cells, LCV trafficking and substrate translocation. LpnE belongs to a subfamily of tetratricopeptide repeat proteins known as Sel1-like repeats (SLRs). All eight of the predicted SLRs in LpnE are required to promote host cell invasion. Herein, we report that LpnE(1-375) localizes to cis-Golgi in HEK293 cells via its signal peptide (aa 1-22). We further verify the interaction of LpnE(73-375) and LpnE(22-375) with Oculocerebrorenal syndrome of Lowe protein (OCRL) residues 10-208, restricting the known interacting residues for both proteins. To further characterize the SLR region of LpnE, we solved the crystal structure of LpnE(73-375) to 1.75A resolution. This construct comprises all SLRs, which are arranged in a super-helical fold. The alpha-helices forming the inner concave surface of the LpnE super-helix suggest a potential protein-protein interaction interface. This article is protected by copyright. All rights reserved. The structure of Legionella effector protein LpnE provides insights into its interaction with Oculocerebrorenal syndrome of Lowe (OCRL) protein.,Voth K, Chung IYW, van Straaten K, Li L, Boniecki MT, Cygler M FEBS J. 2018 Nov 26. doi: 10.1111/febs.14710. PMID:30479037 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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