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@ARTICLE{Flacht:602297,
      author       = {Flacht, Lara and Lunelli, Michele and Kaszuba, Karol and
                      Chen, Zhuo Angel and Reilly, Francis J. O'. and Rappsilber,
                      Juri and Kosinski, Jan and Kolbe, Michael},
      title        = {{I}ntegrative structural analysis of the type {III}
                      secretion system needle complex from {S}higella flexneri},
      journal      = {Protein science},
      volume       = {32},
      number       = {4},
      issn         = {0961-8368},
      address      = {Bethesda, Md.},
      publisher    = {Protein Society},
      reportid     = {PUBDB-2024-00572},
      pages        = {e4595},
      year         = {2023},
      note         = {Supported by the UHH and DFG grant numbers (INST
                      152/772-1|152/774-1|152/775-1|152/776-1|152/777-1 FUGG).},
      abstract     = {The type III secretion system (T3SS) is a large,
                      transmembrane protein machinery used by various pathogenic
                      gram-negative bacteria to transport virulence factors into
                      the host cell during infection. Understanding the structure
                      of T3SSs is crucial for future developments of therapeutics
                      that could target this system. However, much of the
                      knowledge about the structure of T3SS is available only for
                      Salmonella, and it is unclear how this large assembly is
                      conserved across species. Here, we combined cryo-electron
                      microscopy, cross-linking mass spectrometry, and integrative
                      modeling to determine the structure of the T3SS needle
                      complex from Shigella flexneri. We show that the Shigella
                      T3SS exhibits unique features distinguishing it from other
                      structurally characterized T3SSs. The secretin pore complex
                      adopts a new fold of its C-terminal S domain and the pilotin
                      MxiM[SctG] locates around the outer surface of the pore. The
                      export apparatus structure exhibits a conserved
                      pseudohelical arrangement but includes the N-terminal domain
                      of the SpaS[SctU] subunit, which was not present in any of
                      the previously published virulence-related T3SS structures.
                      Similar to other T3SSs, however, the apparatus is anchored
                      within the needle complex by a network of flexible linkers
                      that either adjust conformation to connect to equivalent
                      patches on the secretin oligomer or bind distinct surface
                      patches at the same height of the export apparatus. The
                      conserved and unique features delineated by our analysis
                      highlight the necessity to analyze T3SS in a
                      species-specific manner, in order to fully understand the
                      underlying molecular mechanisms of these systems. The
                      structure of the type III secretion system from Shigella
                      flexneri delineates conserved and unique features, which
                      could be used for the development of broad-range
                      therapeutics.},
      cin          = {CSSB-EMBL-JK / CSSB-HZI-MK},
      ddc          = {610},
      cid          = {I:(DE-H253)CSSB-EMBL-JK-20210701 /
                      I:(DE-H253)CSSB-HZI-MK-20210520},
      pnm          = {899 - ohne Topic (POF4-899)},
      pid          = {G:(DE-HGF)POF4-899},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:36790757},
      UT           = {WOS:000950175300001},
      doi          = {10.1002/pro.4595},
      url          = {https://bib-pubdb1.desy.de/record/602297},
}