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@ARTICLE{Junglas:1006880,
      author       = {Junglas, Benedikt and Gewehr, Lucas and Jilly, Ruven and
                      Franz, Johannes and Zu, Whenju Eva and Weidner, Tobias and
                      Bonn, Mischa and Sachse, Carsten and Schneider, Dirk},
      title        = {{S}yn{DLP} is a dynamin-like protein of {S}ynechocystis sp.
                      {PCC} 6803 with eukaryotic features},
      journal      = {Nature Communications},
      volume       = {14},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {FZJ-2023-01912},
      pages        = {2156},
      year         = {2023},
      abstract     = {Dynamin-like proteins are membrane remodeling GTPases with
                      well-understood functions in eukaryotic cells. However,
                      bacterial dynamin-like proteins are still poorly
                      investigated. SynDLP, the dynamin-like protein of the
                      cyanobacterium Synechocystis sp. PCC 6803, forms ordered
                      oligomers in solution. The 3.7 Å resolution cryo-EM
                      structure of SynDLP oligomers reveals the presence of
                      oligomeric stalk interfaces typical for eukaryotic
                      dynamin-like proteins. The bundle signaling element domain
                      shows distinct features, such as an intramolecular disulfide
                      bridge that affects the GTPase activity, or an expanded
                      intermolecular interface with the GTPase domain. In addition
                      to typical GD-GD contacts, such atypical GTPase domain
                      interfaces might be a GTPase activity regulating tool in
                      oligomerized SynDLP. Furthermore, we show that SynDLP
                      interacts with and intercalates into membranes containing
                      negatively charged thylakoid membrane lipids independent of
                      nucleotides. The structural characteristics of SynDLP
                      oligomers suggest it to be the closest known bacterial
                      ancestor of eukaryotic dynamin.},
      cin          = {ER-C-3},
      ddc          = {500},
      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       = {37059718},
      UT           = {WOS:000969250300022},
      doi          = {10.1038/s41467-023-37746-9},
      url          = {https://juser.fz-juelich.de/record/1006880},
}