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@ARTICLE{Legewie:873653,
      author       = {Legewie, Larissa and Loschwitz, Jennifer and Steffens, Nora
                      and Prescher, Martin and Wang, Xue and Smits, Sander H. J.
                      and Schmitt, Lutz and Strodel, Birgit and Degrandi, Daniel
                      and Pfeffer, Klaus},
      title        = {{B}iochemical and structural characterization of murine
                      {GBP}7, a guanylate binding protein with an elongated
                      {C}-terminal tail},
      journal      = {Biochemical journal},
      volume       = {476},
      number       = {21},
      issn         = {1470-8728},
      address      = {London},
      publisher    = {Portland Press79505},
      reportid     = {FZJ-2020-00884},
      pages        = {3161 - 3182},
      year         = {2019},
      abstract     = {Guanylate-binding proteins (GBPs) constitute a family of
                      interferon-inducible guanosine triphosphatases (GTPases)
                      that are key players in host defense against intracellular
                      pathogens ranging from protozoa to bacteria and viruses. So
                      far, human GBP1 and GBP5 as well as murine GBP2 (mGBP2) have
                      been biochemically characterized in detail. Here, with
                      murine GBP7 (mGBP7), a GBP family member with an
                      unconventional and elongated C-terminus is analyzed. The
                      present study demonstrates that mGBP7 exhibits a
                      concentration-dependent GTPase activity and an apparent GTP
                      turnover number of 20 min-1. In addition, fluorescence
                      spectroscopy analyses reveal that mGBP7 binds GTP with high
                      affinity (KD = 0.22 µM) and GTPase activity assays
                      indicate that mGBP7 hydrolyzes GTP to GDP and GMP. The mGBP7
                      GTPase activity is inhibited by incubation with γ-phosphate
                      analogs and a K51A mutation interfering with GTP binding.
                      SEC-MALS analyses give evidence that mGBP7 forms transient
                      dimers and that this oligomerization pattern is not
                      influenced by the presence of nucleotides. Moreover, a
                      structural model for mGBP7 is provided by homology modeling,
                      which shows that the GTPase possesses an elongated
                      C-terminal (CT) tail compared with the CaaX motif-containing
                      mGBP2 and human GBP1. Molecular dynamics simulations
                      indicate that this tail has transmembrane characteristics
                      and, interestingly, confocal microscopy analyses reveal that
                      the CT tail is required for recruitment of mGBP7 to the
                      parasitophorous vacuole of Toxoplasma gondii.},
      cin          = {ICS-6 / JARA-HPC},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-6-20110106 / $I:(DE-82)080012_20140620$},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551) /
                      Structural dynamics of murine guanylate binding proteins,
                      their dimerization and interaction with lipid bilayers
                      $(jics6a_20190501)$},
      pid          = {G:(DE-HGF)POF3-551 / $G:(DE-Juel1)jics6a_20190501$},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31689351},
      UT           = {WOS:000509877500004},
      doi          = {10.1042/BCJ20190364},
      url          = {https://juser.fz-juelich.de/record/873653},
}