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10.7554/eLife.23644 http://scihub22266oqcxt.onion/10.7554/eLife.23644 C5437283!5437283!28323617     free     free     free Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       eLife 2017 ; 6 (ä): ä Nephropedia Template TP {{tp|p=28323617|t=2017. CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin |pdf=|usr=}}{{28323617}} gab.com Text CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin JO: eLife http://www.kidney.de/pget.php?&tw=1&pmid=28323617 #FOAvip Many pathogenic bacteria produce pore-forming toxins to attack and kill human cells. We have determined the 4.5 Å structure of the ~2.2 MDa pore complex of pneumolysin, the main virulence factor of Streptococcus pneumoniae, by cryoEM. The pneumolysin pore is a 400 Å ring of 42 membrane-inserted monomers. Domain 3 of the soluble toxin refolds into two ~85 Å ?-hairpins that traverse the lipid bilayer and assemble into a 168-strand ?-barrel. The pore complex is stabilized by salt bridges between ?-hairpins of adjacent subunits and an internal ?-barrel. The apolar outer barrel surface with large sidechains is immersed in the lipid bilayer, while the inner barrel surface is highly charged. Comparison of the cryoEM pore complex to the prepore structure obtained by electron cryo-tomography and the x-ray structure of the soluble form reveals the detailed mechanisms by which the toxin monomers insert into the lipid bilayer to perforate the target membrane.DOI:http://dx.doi.org/10.7554/eLife.23644.001 Twit Text FOAVip CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin ????eLife http://www.kidney.de/pget.php?&tw=1&pmid=28323617 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28323617 #FOAvip English Wikipedia <ref>{{Cite pmid|28323617}}</ref> CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin #MMPMID28323617 van Pee K; Neuhaus A; D'Imprima E; Mills DJ; Kühlbrandt W; Yildiz Ö eLife 2017[]; 6 (ä): ä PMID28323617show ga Many pathogenic bacteria produce pore-forming toxins to attack and kill human cells. We have determined the 4.5 Å structure of the ~2.2 MDa pore complex of pneumolysin, the main virulence factor of Streptococcus pneumoniae, by cryoEM. The pneumolysin pore is a 400 Å ring of 42 membrane-inserted monomers. Domain 3 of the soluble toxin refolds into two ~85 Å ?-hairpins that traverse the lipid bilayer and assemble into a 168-strand ?-barrel. The pore complex is stabilized by salt bridges between ?-hairpins of adjacent subunits and an internal ?-barrel. The apolar outer barrel surface with large sidechains is immersed in the lipid bilayer, while the inner barrel surface is highly charged. Comparison of the cryoEM pore complex to the prepore structure obtained by electron cryo-tomography and the x-ray structure of the soluble form reveals the detailed mechanisms by which the toxin monomers insert into the lipid bilayer to perforate the target membrane.DOI:http://dx.doi.org/10.7554/eLife.23644.001 äCryoEM structures of membrane pore and prepore complex reveal cytolyti(epmc).pdf DeepDyve Pubget Overpricing