4fgo

Legionella pneumophila LapG (calcium-bound)

spinqualitylabelsall models 4fgo, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4fgo is a 1 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 1.903Å Ligands: CA, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5ZXA4_LEGPH Publication Abstract from PubMed The bacterial dinucleotide second messenger c-di-GMP has emerged as a central molecule in regulating bacterial behavior, including motility and biofilm formation. Proteins for the synthesis and degradation of c-di-GMP and effectors for its signal transmission are widely used in the bacterial domain. Previous work established the GGDEF-EAL domain-containing receptor LapD as a central switch in Pseudomonas fluorescens cell adhesion. LapD senses c-di-GMP inside the cytosol and relays this signal to the outside by the differential recruitment of the periplasmic protease LapG. Here we identify the core components of an orthologous system in Legionella pneumophila. Despite only moderate sequence conservation at the protein level, key features concerning the regulation of LapG are retained. The output domain of the LapD-like receptor from L. pneumophila, CdgS9, binds the LapG ortholog involving a strictly conserved surface tryptophan residue. While the endogenous substrate for L. pneumophila LapG is unknown, the enzyme processed the corresponding P. fluorescens substrate, indicating a common catalytic mechanism and substrate recognition. Crystal structures of L. pneumophila LapG provide the first atomic models of bacterial proteases of the DUF920 family and reveal a conserved calcium-binding site important for LapG function. Structural characterization of a conserved, calcium-dependent periplasmic protease from Legionella pneumophila.,Chatterjee D, Boyd CD, O'Toole GA, Sondermann H J Bacteriol. 2012 Aug;194(16):4415-25. doi: 10.1128/JB.00640-12. Epub 2012 Jun, 15. PMID:22707706 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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