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10.1038/srep14352 http://scihub22266oqcxt.onion/10.1038/srep14352 C4585913!4585913 !26403197     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26403197 &cmd=llinks): Failed to open stream: HTTP request failed! 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Crystal structure of Streptococcus pneumoniae pneumolysin provides key insights into early steps of pore formation |pdf=|usr=}}{{26403197 }} gab.com Text Crystal structure of Streptococcus pneumoniae pneumolysin provides key insights into early steps of pore formation JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=26403197 #FOAvip Pore-forming proteins are weapons often used by bacterial pathogens to breach the membrane barrier of target cells. Despite their critical role in infection important structural aspects of the mechanism of how these proteins assemble into pores remain unknown. Streptococcus pneumoniae is the world's leading cause of pneumonia, meningitis, bacteremia and otitis media. Pneumolysin (PLY) is a major virulence factor of S. pneumoniae and a target for both small molecule drug development and vaccines. PLY is a member of the cholesterol-dependent cytolysins (CDCs), a family of pore-forming toxins that form gigantic pores in cell membranes. Here we present the structure of PLY determined by X-ray crystallography and, in solution, by small-angle X-ray scattering. The crystal structure reveals PLY assembles as a linear oligomer that provides key structural insights into the poorly understood early monomer-monomer interactions of CDCs at the membrane surface. Twit Text FOAVip Crystal structure of Streptococcus pneumoniae pneumolysin provides key insights into early steps of pore formation ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=26403197 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26403197 #FOAvip English Wikipedia <ref>{{Cite pmid|26403197 }}</ref> Crystal structure of Streptococcus pneumoniae pneumolysin provides key insights into early steps of pore formation #MMPMID26403197 Lawrence SL ; Feil SC ; Morton CJ ; Farrand AJ ; Mulhern TD ; Gorman MA ; Wade KR ; Tweten RK ; Parker MW Sci Rep 2015[Sep]; 5 (ä): 14352 PMID26403197 show ga Pore-forming proteins are weapons often used by bacterial pathogens to breach the membrane barrier of target cells. Despite their critical role in infection important structural aspects of the mechanism of how these proteins assemble into pores remain unknown. Streptococcus pneumoniae is the world's leading cause of pneumonia, meningitis, bacteremia and otitis media. Pneumolysin (PLY) is a major virulence factor of S. pneumoniae and a target for both small molecule drug development and vaccines. PLY is a member of the cholesterol-dependent cytolysins (CDCs), a family of pore-forming toxins that form gigantic pores in cell membranes. Here we present the structure of PLY determined by X-ray crystallography and, in solution, by small-angle X-ray scattering. The crystal structure reveals PLY assembles as a linear oligomer that provides key structural insights into the poorly understood early monomer-monomer interactions of CDCs at the membrane surface. |*Models, Molecular [MESH] |*Protein Conformation [MESH] |Bacterial Proteins/chemistry/genetics/metabolism [MESH] |Binding Sites [MESH] |Carbohydrates/chemistry [MESH] |Crystallography, X-Ray [MESH] |Mannose/metabolism [MESH] |Molecular Docking Simulation [MESH] |Mutation [MESH] |Protein Binding [MESH] |Protein Multimerization [MESH] |Solutions [MESH] |Streptolysins/*chemistry/genetics/metabolism [MESH]Crystal structure of Streptococcus pneumoniae pneumolysin provides key(epmc).pdf DeepDyve Pubget Overpricing