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@ARTICLE{Lunelli:602316,
      author       = {Lunelli, Michele and Kamprad, Antje and Bürger, Jörg and
                      Mielke, Thorsten and Spahn, Christian M. T. and Kolbe,
                      Michael},
      title        = {{C}ryo-{EM} structure of the {S}higella type {III} needle
                      complex},
      journal      = {PLoS pathogens},
      volume       = {16},
      number       = {2},
      issn         = {1553-7366},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {PUBDB-2024-00591},
      pages        = {e1008263},
      year         = {2020},
      abstract     = {The Type III Secretion Systems (T3SS) needle complex is a
                      conserved syringe-shaped protein translocation nanomachine
                      with a mass of about 3.5 MDa essential for the survival and
                      virulence of many Gram-negative bacterial pathogens. This
                      system is composed of a membrane-embedded basal body and an
                      extracellular needle that deliver effector proteins into
                      host cells. High-resolution structures of the T3SS from
                      different organisms and infection stages are needed to
                      understand the underlying molecular mechanisms of effector
                      translocation. Here, we present the cryo-electron microscopy
                      structure of the isolated Shigella T3SS needle complex. The
                      inner membrane (IM) region of the basal body adopts 24-fold
                      rotational symmetry and forms a channel system that connects
                      the bacterial periplasm with the export apparatus cage. The
                      secretin oligomer adopts a heterogeneous architecture with
                      16- and 15-fold cyclic symmetry in the periplasmic
                      N-terminal connector and C-terminal outer membrane ring,
                      respectively. Two out of three IM subunits bind the secretin
                      connector via a β-sheet augmentation. The cryo-EM map also
                      reveals the helical architecture of the export apparatus
                      core, the inner rod, the needle and their intervening
                      interfaces.},
      cin          = {CSSB-HZI-MK},
      ddc          = {610},
      cid          = {I:(DE-H253)CSSB-HZI-MK-20210520},
      pnm          = {899 - ohne Topic (POF4-899) / iNEXT - Infrastructure for
                      NMR, EM and X-rays for translational research (653706) /
                      FUTURE T3SS - Bacterial effector secretion: Function and
                      Architecture of the Type 3 Secretion System (311374)},
      pid          = {G:(DE-HGF)POF4-899 / G:(EU-Grant)653706 /
                      G:(EU-Grant)311374},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32092125},
      UT           = {WOS:000518637800012},
      doi          = {10.1371/journal.ppat.1008263},
      url          = {https://bib-pubdb1.desy.de/record/602316},
}