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@ARTICLE{Hollenstein:300896,
      author       = {Hollenstein, Kaspar and Comellas-Bigler, Mireia and Bevers,
                      Loes E. and Feiters, Martin C. and Meyer-Klaucke, Wolfram
                      and Hagedoorn, Peter-Leon and Locher, Kaspar P.},
      title        = {{D}istorted octahedral coordination of tungstate in a
                      subfamily of specific binding proteins},
      journal      = {Journal of biological inorganic chemistry},
      volume       = {14},
      number       = {5},
      issn         = {1432-1327},
      address      = {Berlin},
      publisher    = {Springer},
      reportid     = {PUBDB-2016-02463},
      pages        = {663 - 672},
      year         = {2009},
      note         = {(c) SBIC},
      abstract     = {Bacteria and archaea import molybdenum andtungsten from the
                      environment in the form of theoxyanions molybdate (MoO42-)
                      and tungstate (WO42-).These substrates are captured by an
                      external, high-affinitybinding protein, and delivered to ATP
                      binding cassettetransporters, which move them across the
                      cell membrane.We have recently reported a crystal structure
                      of themolybdate/tungstate binding protein ModA/WtpA
                      fromArchaeoglobus fulgidus, which revealed an
                      octahedrallycoordinated central metal atom. By contrast, the
                      previouslydetermined structures of three bacterial homologs
                      showedtetracoordinate molybdenum and tungsten atoms in
                      theirbinding pockets. Until then, coordination numbers
                      abovefour had only been found for molybdenum/tungsten
                      inmetalloenzymes where these metal atoms are part of
                      thecatalytic cofactors and coordinated by mostly
                      non-oxygenligands. We now report a high-resolution structure
                      ofA. fulgidus ModA/WtpA, as well as crystal structures
                      offour additional homologs, all bound to tungstate.
                      Thesecrystal structures match X-ray absorption
                      spectroscopymeasurements from soluble, tungstate-bound
                      protein, andreveal the details of the distorted octahedral
                      coordination.Our results demonstrate that the distorted
                      octahedralgeometry is not an exclusive feature of the A.
                      fulgidusprotein, and suggest distinct binding modes of the
                      bindingproteins from archaea and bacteria.},
      cin          = {EMBL / EMBL-User},
      ddc          = {540},
      cid          = {I:(DE-H253)EMBL-20120731 / I:(DE-H253)EMBL-User-20120814},
      pnm          = {899 - ohne Topic (POF3-899)},
      pid          = {G:(DE-HGF)POF3-899},
      experiment   = {EXP:(DE-H253)D-D2-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19234723},
      UT           = {WOS:000266924400003},
      doi          = {10.1007/s00775-009-0479-7},
      url          = {https://bib-pubdb1.desy.de/record/300896},
}