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@ARTICLE{Dietsche:390575,
      author       = {Dietsche, Tobias and Tesfazgi Mebrhatu, Mehari and Brunner,
                      Matthias J. and Abrusci, Patrizia and Yan, Jun and
                      Franz-Wachtel, Mirita and Schärfe, Charlotta and Zilkenat,
                      Susann and Grin, Iwan and Galán, Jorge E. and Kohlbacher,
                      Oliver and Lea, Susan and Macek, Boris and Marlovits, Thomas
                      and Robinson, Carol V. and Wagner, Samuel},
      title        = {{S}tructural and {F}unctional {C}haracterization of the
                      {B}acterial {T}ype {III} {S}ecretion {E}xport {A}pparatus},
      journal      = {PLoS pathogens},
      volume       = {12},
      number       = {12},
      issn         = {1553-7374},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {PUBDB-2017-09658},
      pages        = {e1006071 -},
      year         = {2016},
      abstract     = {Bacterial type III protein secretion systems inject
                      effector proteins into eukaryotic host cells in order to
                      promote survival and colonization of Gram-negative pathogens
                      and symbionts. Secretion across the bacterial cell envelope
                      and injection into host cells is facilitated by a so-called
                      injectisome. Its small hydrophobic export apparatus
                      components SpaP and SpaR were shown to nucleate assembly of
                      the needle complex and to form the central “cup”
                      substructure of a Salmonella Typhimurium secretion system.
                      However, the in vivo placement of these components in the
                      needle complex and their function during the secretion
                      process remained poorly defined. Here we present evidence
                      that a SpaP pentamer forms a 15 Å wide pore and provide a
                      detailed map of SpaP interactions with the export apparatus
                      components SpaQ, SpaR, and SpaS. We further refine the
                      current view of export apparatus assembly, consolidate
                      transmembrane topology models for SpaP and SpaR, and present
                      intimate interactions of the periplasmic domains of SpaP and
                      SpaR with the inner rod protein PrgJ, indicating how export
                      apparatus and needle filament are connected to create a
                      continuous conduit for substrate translocation.},
      cin          = {CSSB-UKE},
      ddc          = {610},
      cid          = {I:(DE-H253)CSSB-UKE-20141216},
      pnm          = {6215 - Soft Matter, Health and Life Sciences (POF3-621)},
      pid          = {G:(DE-HGF)POF3-6215},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000392202100046},
      pubmed       = {pmid:27977800},
      doi          = {10.1371/journal.ppat.1006071},
      url          = {https://bib-pubdb1.desy.de/record/390575},
}