{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Spreter T"],"funding":["NIAID NIH HHS","NIGMS NIH HHS"],"pagination":["468-76"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2860953"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(5)"],"pubmed_abstract":["The type III secretion system (T3SS) is a macromolecular 'injectisome' that allows bacterial pathogens to transport virulence proteins into the eukaryotic host cell. This macromolecular complex is composed of connected ring-like structures that span both bacterial membranes. The crystal structures of the periplasmic domain of the outer membrane secretin EscC and the inner membrane protein PrgH reveal the conservation of a modular fold among the three proteins that form the outer membrane and inner membrane rings of the T3SS. This leads to the hypothesis that this conserved fold provides a common ring-building motif that allows for the assembly of the variably sized outer membrane and inner membrane rings characteristic of the T3SS. Using an integrated structural and experimental approach, "],"journal":["Nature structural & molecular biology"],"pubmed_title":["A conserved structural motif mediates formation of the periplasmic rings in the type III secretion system."],"pmcid":["PMC2860953"],"funding_grant_id":["P20 GM076222","R01 AI030479","U54 AI057141","U54 AI05741"],"pubmed_authors":["Spreter T","Kimbrough TG","Baker D","Pfuetzner RA","Miller SI","Vuckovic M","Strynadka NC","Yip CK","Andre I","Sanowar S","Deng W","Yu AC","Finlay BB"],"additional_accession":[]},"is_claimable":false,"name":"A conserved structural motif mediates formation of the periplasmic rings in the type III secretion system.","description":"The type III secretion system (T3SS) is a macromolecular 'injectisome' that allows bacterial pathogens to transport virulence proteins into the eukaryotic host cell. This macromolecular complex is composed of connected ring-like structures that span both bacterial membranes. The crystal structures of the periplasmic domain of the outer membrane secretin EscC and the inner membrane protein PrgH reveal the conservation of a modular fold among the three proteins that form the outer membrane and inner membrane rings of the T3SS. This leads to the hypothesis that this conserved fold provides a common ring-building motif that allows for the assembly of the variably sized outer membrane and inner membrane rings characteristic of the T3SS. Using an integrated structural and experimental approach, ","dates":{"release":"2009-01-01T00:00:00Z","publication":"2009 May","modification":"2026-05-04T10:58:04.372Z","creation":"2019-03-27T00:30:24Z"},"accession":"S-EPMC2860953","cross_references":{"pubmed":["19396170"],"doi":["10.1038/nsmb.1603"]}}