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@ARTICLE{Myllykoski:168209,
      author       = {Myllykoski, Matti and Raasakka, Arne and Lehtimäki, Mari
                      and Han, Huijong and Kursula, Inari and Kursula, Petri},
      title        = {{C}rystallographic {A}nalysis of the {R}eaction {C}ycle of
                      2′,3′-{C}yclic {N}ucleotide 3′-{P}hosphodiesterase, a
                      {U}nique {M}ember of the 2{H} {P}hosphoesterase {F}amily},
      journal      = {Journal of molecular biology},
      volume       = {425},
      number       = {22},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {DESY-2014-02414},
      pages        = {4307 - 4322},
      year         = {2013},
      note         = {© Elsevier Ltd.; Post referee fulltext in progress;
                      Embargo 12 months from publication},
      abstract     = {2H phosphoesterases catalyze reactions on nucleotide
                      substrates and contain two conserved histidine residues in
                      the active site. Very limited information is currently
                      available on the details of the active site and
                      substrate/product binding during the catalytic cycle of
                      these enzymes. We performed a comprehensive X-ray
                      crystallographic study of mouse 2',3'-cyclic nucleotide
                      3'-phosphodiesterase (CNPase), a membrane-associated enzyme
                      present at high levels in the tetrapod myelin sheath. We
                      determined crystal structures of the CNPase
                      phosphodiesterase domain complexed with substrate, product,
                      and phosphorothioate analogues. The data provide detailed
                      information on the CNPase reaction mechanism, including
                      substrate binding mode and coordination of the nucleophilic
                      water molecule. Linked to the reaction, an open/close motion
                      of the β5-α7 loop is observed. The role of the N terminus
                      of helix α7--unique for CNPase in the 2H family--during the
                      reaction indicates that 2H phosphoesterases differ in their
                      respective reaction mechanisms despite the conserved
                      catalytic residues. Furthermore, based on small-angle X-ray
                      scattering, we present a model for the full-length enzyme,
                      indicating that the two domains of CNPase form an elongated
                      molecule. Finally, based on our structural data and a
                      comprehensive bioinformatics study, we discuss the
                      conservation of CNPase in various organisms.},
      cin          = {EMBL-User},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {DORIS Beamline K1.1 (POF2-54G13) / PETRA Beamline P14
                      (POF2-54G14)},
      pid          = {G:(DE-H253)POF2-K1.1-20130405 /
                      G:(DE-H253)POF2-P14-20130405},
      experiment   = {EXP:(DE-H253)D-K1.1-20150101 / EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000328100500023},
      pubmed       = {pmid:23831225},
      doi          = {10.1016/j.jmb.2013.06.012},
      url          = {https://bib-pubdb1.desy.de/record/168209},
}