3bws

Crystal structure of the leptospiral antigen Lp49

spinqualitylabelsall models 3bws, resolution 1.99Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3bws is a 2 chain structure with sequence from Leptospira interrogans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.99Å Ligands: MSE, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LP49_LEPIC May be involved in virulence. Binds human plasminogen (PLG) and stimulates its proteolytic cleavage to enzymatically active plasmin in the presence of an urokinase-type PLG activator in vitro. Activated plasmin has proteolytic activity which may help the bacteria to spread throughout the host by degrading extracellular matrix components, facilitating tissue penetration and invasion. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Pathogenic Leptospira is the etiological agent of leptospirosis, a life-threatening disease that affects populations worldwide. Currently available vaccines have limited effectiveness and therapeutic interventions are complicated by the difficulty in making an early diagnosis of leptospirosis. The genome of Leptospira interrogans was recently sequenced and comparative genomic analysis contributed to the identification of surface antigens, potential candidates for development of new vaccines and serodiagnosis. Lp49 is a membrane-associated protein recognized by antibodies present in sera from early and convalescent phases of leptospirosis patients. Its crystal structure was determined by single-wavelength anomalous diffraction using selenomethionine-labelled crystals and refined at 2.0 A resolution. Lp49 is composed of two domains and belongs to the all-beta-proteins class. The N-terminal domain folds in an immunoglobulin-like beta-sandwich structure, whereas the C-terminal domain presents a seven-bladed beta-propeller fold. Structural analysis of Lp49 indicates putative protein-protein binding sites, suggesting a role in Leptospira-host interaction. This is the first crystal structure of a leptospiral antigen described to date. The leptospiral antigen Lp49 is a two-domain protein with putative protein binding function.,Giuseppe PO, Neves FO, Nascimento AL, Guimaraes BG J Struct Biol. 2008 Jul;163(1):53-60. Epub 2008 Apr 14. PMID:18508281 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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