5bq9

Crystal structure of uncharacterized protein lpg1496 Legionella pneumophila subsp. pneumophila

spinqualitylabelsall models 5bq9, resolution 2.28Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5bq9 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 2.2785Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5ZVE4_LEGPH Publication Abstract from PubMed Legionella pneumophila, the intracellular pathogen that can cause severe pneumonia known as Legionnaire's disease, translocates close to 300 effectors inside the host cell using Dot/Icm type IVB secretion system. The structure and function for the majority of these effector proteins remains unknown. Here, we present the crystal structure of the L. pneumophila effector Lem10. The structure reveals a multidomain organization with the largest C-terminal domain showing strong structural similarity to the HD protein superfamily representatives. However, Lem10 lacks the catalytic His-Asp residue pair and does not show any in vitro phosphohydrolase enzymatic activity, typical for HD proteins. While the biological function of Lem10 remains elusive, our analysis shows that similar distinct features are shared by a significant number of HD domains found in Legionella proteins, including the SidE family of effectors known to play an important role during infection. Taken together our data point to the presence of a specific group of non-catalytic Legionella HD domains, dubbed LHDs, which are involved in pathogenesis. Proteins 2015;. (c) 2015 Wiley Periodicals, Inc. Crystal structure of the Legionella pneumophila lem10 effector reveals a new member of the HD protein superfamily.,Morar M, Evdokimova E, Chang C, Ensminger AW, Savchenko A Proteins. 2015 Oct 1. doi: 10.1002/prot.24933. PMID:26426142 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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