% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Junglas:1030511,
      author       = {Junglas, Benedikt and Gewehr, Lucas and Mernberger, Lara
                      and Schönnenbeck, Philipp and Jilly, Ruven and Hellmann,
                      Nadja and Schneider, Dirk and Sachse, Carsten},
      title        = {{S}tructural basis for {GTP}ase activity and conformational
                      changes of the bacterial dynamin-like protein {S}yn{DLP}},
      journal      = {Cell reports},
      volume       = {43},
      number       = {9},
      issn         = {2211-1247},
      address      = {[New York, NY]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2024-05334},
      pages        = {114657 -},
      year         = {2024},
      abstract     = {SynDLP, a dynamin-like protein (DLP) encoded in the
                      cyanobacterium Synechocystis sp. PCC 6803, has recently been
                      identified to be structurally highly similar to eukaryotic
                      dynamins. To elucidate structural changes during guanosine
                      triphosphate (GTP) hydrolysis, we solved the cryoelectron
                      microscopy (cryo-EM) structures of oligomeric full-length
                      SynDLP after addition of guanosine diphosphate (GDP) at 4.1
                      Å and GTP at 3.6-Å resolution as well as a GMPPNP-bound
                      dimer structure of a minimal G-domain construct of SynDLP at
                      3.8-Å resolution. In comparison with what has been seen in
                      the previously resolved apo structure, we found that the
                      G-domain is tilted upward relative to the stalk upon GTP
                      hydrolysis and that the G-domain dimerizes via an additional
                      extended dimerization domain not present in canonical
                      G-domains. When incubated with lipid vesicles, we observed
                      formation of irregular tubular SynDLP assemblies that
                      interact with negatively charged lipids. Here, we provide
                      the structural framework of a series of different functional
                      SynDLP assembly states during GTP turnover.},
      cin          = {ER-C-3},
      ddc          = {610},
      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       = {39207903},
      UT           = {WOS:001316475700001},
      doi          = {10.1016/j.celrep.2024.114657},
      url          = {https://juser.fz-juelich.de/record/1030511},
}