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@ARTICLE{Junglas:1030409,
      author       = {Junglas, Benedikt and Hudina, Esther and Schönnenbeck,
                      Philipp and Ritter, Ilona and Heddier, Anja and
                      Santiago-Schübel, Beatrix and Huesgen, Pitter F. and
                      Schneider, Dirk and Sachse, Carsten},
      title        = {{S}tructural plasticity of bacterial {ESCRT}-{III} protein
                      {P}sp{A} in higher-order assemblies},
      journal      = {Nature structural $\&$ molecular biology},
      volume       = {32},
      issn         = {1545-9993},
      address      = {London [u.a.]},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2024-05282},
      pages        = {23-34},
      year         = {2025},
      abstract     = {Eukaryotic members of the endosome sorting complex required
                      for transport-III (ESCRT-III) family have been shown to form
                      diverse higher-order assemblies. The bacterial phage shock
                      protein A (PspA) has been identified as a member of the
                      ESCRT-III superfamily, and PspA homo-oligomerizes to form
                      rod-shaped assemblies. As observed for eukaryotic ESCRT-III,
                      PspA forms tubular assemblies of varying diameters. Using
                      electron cryo-electron microscopy, we determined 61
                      Synechocystis PspA structures and observed in molecular
                      detail how the structural plasticity of PspA rods is
                      mediated by conformational changes at three hinge regions in
                      the monomer and by the fixed and changing molecular contacts
                      between protomers. Moreover, we reduced and increased the
                      structural plasticity of PspA rods by removing the loop
                      connecting helices α3/α4 and the addition of nucleotides,
                      respectively. Based on our analysis of PspA-mediated
                      membrane remodeling, we suggest that the observed mode of
                      structural plasticity is a prerequisite for the biological
                      function of ESCRT-III members.},
      cin          = {ER-C-3},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ER-C-3-20170113},
      pnm          = {5352 - Understanding the Functionality of Soft Matter and
                      Biomolecular Systems (POF4-535) / 5241 - Molecular
                      Information Processing in Cellular Systems (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5352 / G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {39152237},
      UT           = {WOS:001292655700003},
      doi          = {10.1038/s41594-024-01359-7},
      url          = {https://juser.fz-juelich.de/record/1030409},
}