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@ARTICLE{Yuan:603155,
      author       = {Yuan, Biao and Scholz, Jonas and Wald, Jiri and Thünauer,
                      Roland and Hennell James, Rory and Ellenberg, Irina and
                      Windhorst, Sabine and Faix, Jan and Marlovits, Thomas},
      title        = {{S}tructural basis for subversion of host cell actin
                      cytoskeleton during {S}almonella infection},
      journal      = {Science advances},
      volume       = {9},
      number       = {49},
      issn         = {2375-2548},
      address      = {Washington, DC [u.a.]},
      publisher    = {Assoc.},
      reportid     = {PUBDB-2024-00792},
      pages        = {eadj5777},
      year         = {2023},
      note         = {DFG Fa330/12-3. Part of this work was performed at the
                      Multi-User Cryo-EM Facility at the Centre for Structural
                      Systems Biology, Hamburg, supported by the University of
                      Hamburg and DFG grant numbers (INST 152/772-1, 152/774-1,
                      152/775-1, 152/776-1, and 152/777-1 FUGG).},
      abstract     = {Secreted bacterial type III secretion system (T3SS)
                      proteins are essential for successful infection by many
                      human pathogens. Both T3SS translocator SipC and effector
                      SipA are critical for Salmonella infection by subversion of
                      the host cell cytoskeleton, but the precise molecular
                      interplay between them remains unknown. Here, using
                      cryo–electron microscopy, we show that SipA binds along
                      the F-actin grooves with a unique binding pattern. SipA
                      stabilizes F-actin through charged interface residues and
                      appears to prevent inorganic phosphate release through
                      closure of the “back door” of adenosine
                      5′-triphosphate pocket. We also show that SipC enhances
                      the binding of SipA to F-actin, thus demonstrating that a
                      sequential presence of T3SS proteins in host cells is
                      associated with a sequence of infection events—starting
                      with actin nucleation, filament growth, and stabilization.
                      Together, our data explain the coordinated interplay of a
                      precisely tuned and highly effective mechanism during
                      Salmonella infection and provide a blueprint for interfering
                      with Salmonella effectors acting on actin.},
      cin          = {CSSB-UKE-TM / CSSB-CF-ALFM},
      ddc          = {500},
      cid          = {I:(DE-H253)CSSB-UKE-TM-20210520 /
                      I:(DE-H253)CSSB-CF-ALFM-20210629},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633)},
      pid          = {G:(DE-HGF)POF4-633},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:38064550},
      UT           = {WOS:001184467200006},
      doi          = {10.1126/sciadv.adj5777},
      url          = {https://bib-pubdb1.desy.de/record/603155},
}