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@ARTICLE{Nogly:186128,
      author       = {Nogly, Przemyslaw and Gushchin, Ivan and Remeeva, Alina and
                      Esteves, Ana M. and Borges, Nuno and Ma, Pikyee and
                      Ishchenko, Andrii and Grudinin, Sergei and Round, Ekaterina
                      and Moraes, Isabel and Borshchevskiy, Valentin and Santos,
                      Helena and Gordeliy, Valentin and Archer, Margarida},
      title        = {{X}-ray structure of a {CDP}-alcohol
                      phosphatidyltransferase membrane enzyme and insights into
                      its catalytic mechanism},
      journal      = {Nature Communications},
      volume       = {5},
      issn         = {2041-1723},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2015-00216},
      pages        = {1-10},
      year         = {2014},
      abstract     = {Phospholipids have major roles in the structure and
                      function of all cell membranes. Most integral membrane
                      proteins from the large CDP-alcohol phosphatidyltransferase
                      family are involved in phospholipid biosynthesis across the
                      three domains of life. They share a conserved sequence
                      pattern and catalyse the displacement of CMP from a
                      CDP-alcohol by a second alcohol. Here we report the crystal
                      structure of a bifunctional enzyme comprising a cytoplasmic
                      nucleotidyltransferase domain (IPCT) fused with a membrane
                      CDP-alcohol phosphotransferase domain (DIPPS) at 2.65Å
                      resolution. The bifunctional protein dimerizes through the
                      DIPPS domains, each comprising six transmembrane a-helices.
                      The active site cavity is hydrophilic and widely open to the
                      cytoplasm with a magnesium ion surrounded by four highly
                      conserved aspartate residues from helices TM2 and TM3. We
                      show that magnesium is essential for the enzymatic activity
                      and is involved in catalysis. Substrates docking is
                      validated by mutagenesis studies, and a structure-based
                      catalytic mechanism is proposed.},
      cin          = {ICS-6},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000338838500025},
      pubmed       = {pmid:24942835},
      doi          = {10.1038/ncomms5169},
      url          = {https://juser.fz-juelich.de/record/186128},
}