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@ARTICLE{Sajko:453195,
      author       = {Sajko, Sara and Grishkovskaya, Irina and Kostan, Julius and
                      Graewert, Melissa and Setiawan, Kim and Trübestein, Linda
                      and Niedermüller, Korbinian and Gehin, Charlotte and
                      Sponga, Antonio and Puchinger, Martin and Gavin, Anne-Claude
                      and Leonard, Thomas A. and Svergun, Dimitri I. and Smith,
                      Terry K. and Morriswood, Brooke and Djinovic-Carugo,
                      Kristina},
      title        = {{S}tructures of three {MORN} repeat proteins and a
                      re-evaluation of the proposed lipid-binding properties of
                      {MORN} repeats},
      journal      = {PLOS ONE},
      volume       = {15},
      number       = {12},
      issn         = {1932-6203},
      address      = {San Francisco, California, US},
      publisher    = {PLOS},
      reportid     = {PUBDB-2020-05031},
      pages        = {e0242677 -},
      year         = {2020},
      abstract     = {MORN (Membrane Occupation and Recognition Nexus) repeat
                      proteins have a wide taxonomic distribution, being found in
                      both prokaryotes and eukaryotes. Despite this ubiquity, they
                      remain poorly characterised at both a structural and a
                      functional level compared to other common repeats. In
                      functional terms, they are often assumed to be lipid-binding
                      modules that mediate membrane targeting. We addressed this
                      putative activity by focusing on a protein composed solely
                      of MORN repeats—Trypanosoma brucei MORN1. Surprisingly, no
                      evidence for binding to membranes or lipid vesicles by
                      TbMORN1 could be obtained either in vivo or in vitro.
                      Conversely, TbMORN1 did interact with individual
                      phospholipids. High- and low-resolution structures of the
                      MORN1 protein from Trypanosoma brucei and homologous
                      proteins from the parasites Toxoplasma gondii and Plasmodium
                      falciparum were obtained using a combination of
                      macromolecular crystallography, small-angle X-ray
                      scattering, and electron microscopy. This enabled a first
                      structure-based definition of the MORN repeat itself.
                      Furthermore, all three structures dimerised via their
                      C-termini in an antiparallel configuration. The dimers could
                      form extended or V-shaped quaternary structures depending on
                      the presence of specific interface residues. This work
                      provides a new perspective on MORN repeats, showing that
                      they are protein-protein interaction modules capable of
                      mediating both dimerisation and oligomerisation.},
      cin          = {EMBL-User / EMBL},
      ddc          = {610},
      cid          = {I:(DE-H253)EMBL-User-20120814 / I:(DE-H253)EMBL-20120731},
      pnm          = {6G3 - PETRA III (POF3-622)},
      pid          = {G:(DE-HGF)POF3-6G3},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:33296386},
      UT           = {WOS:000598626100043},
      doi          = {10.1371/journal.pone.0242677},
      url          = {https://bib-pubdb1.desy.de/record/453195},
}