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@ARTICLE{Shibazaki:859975,
      author       = {Shibazaki, Chie and Arai, Shigeki and Shimizu, Rumi and
                      Saeki, Morihisa and Kinoshita, Takayoshi and Ostermann,
                      Andreas and Schrader, Tobias E. and Kurosaki, Yuzuru and
                      Sunami, Tomoko and Kuroki, Ryota and Adachi, Motoyasu},
      title        = {{H}ydration {S}tructures of the {H}uman {P}rotein {K}inase
                      {CK}2α {C}larified by {J}oint {N}eutron and {X}-ray
                      {C}rystallography},
      journal      = {Journal of molecular biology},
      volume       = {430},
      number       = {24},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2019-00781},
      pages        = {5094 - 5104},
      year         = {2018},
      abstract     = {Casein kinase 2 (CK2) has broad phosphorylation activity
                      against various regulatory proteins, which are important
                      survival factors in eukaryotic cells. To clarify the
                      hydration structure and catalytic mechanism of CK2, we
                      determined the crystal structure of the alpha subunit of
                      human CK2 containing hydrogen and deuterium atoms using
                      joint neutron (1.9 Å resolution) and X-ray (1.1 Å
                      resolution) crystallography. The analysis revealed the
                      structure of conserved water molecules at the active site
                      and a long potential hydrogen bonding network originating
                      from the catalytic Asp156 that is well known to enhance the
                      nucleophilicity of the substrate OH group to the γ-phospho
                      group of ATP by proton elimination. His148 and Asp214
                      conserved in the protein kinase family are located in the
                      middle of the network. The water molecule forming a hydrogen
                      bond with Asp214 appears to be deformed. In addition,
                      mutational analysis of His148 in CK2 showed significant
                      reductions by $40\%–75\%$ in the catalytic efficiency with
                      similar affinity for ATP. Likewise, remarkable reductions to
                      less than $5\%$ were shown by corresponding mutations on
                      His131 in death-associated protein kinase 1, which belongs
                      to a group different from that of CK2. These findings shed
                      new light on the catalytic mechanism of protein kinases in
                      which the hydrogen bond network through the C-terminal
                      domain may assist the general base catalyst to extract a
                      proton with a link to the bulk solvent via intermediates of
                      a pair of residues.},
      cin          = {JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {610},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6G15 - FRM II / MLZ (POF3-6G15) / 6215 - Soft Matter,
                      Health and Life Sciences (POF3-621) / 6G4 - Jülich Centre
                      for Neutron Research (JCNS) (POF3-623)},
      pid          = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6215 /
                      G:(DE-HGF)POF3-6G4},
      experiment   = {EXP:(DE-MLZ)BIODIFF-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30359582},
      UT           = {WOS:000454377100019},
      doi          = {10.1016/j.jmb.2018.09.018},
      url          = {https://juser.fz-juelich.de/record/859975},
}