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@ARTICLE{Banco:826421,
      author       = {Banco, Michael T. and Mishra, Vidhi and Ostermann, Andreas
                      and Schrader, Tobias E. and Evans, Gary B. and Kovalevsky,
                      Andrey and Ronning, Donald R.},
      title        = {{N}eutron structures of the {H}elicobacter pylori
                      5′-methylthioadenosine nucleosidase highlight proton
                      sharing and protonation states},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {113},
      number       = {48},
      issn         = {1091-6490},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {FZJ-2017-00649},
      pages        = {13756 - 13761},
      year         = {2016},
      abstract     = {MTAN (5′-methylthioadenosine nucleosidase) catalyzes the
                      hydrolysis of the N-ribosidic bond of a variety of
                      adenosine-containing metabolites. The Helicobacter pylori
                      MTAN (HpMTAN) hydrolyzes 6-amino-6-deoxyfutalosine in the
                      second step of the alternative menaquinone biosynthetic
                      pathway. Substrate binding of the adenine moiety is mediated
                      almost exclusively by hydrogen bonds, and the proposed
                      catalytic mechanism requires multiple proton-transfer
                      events. Of particular interest is the protonation state of
                      residue D198, which possesses a pKa above 8 and functions as
                      a general acid to initiate the enzymatic reaction. In this
                      study we present three corefined neutron/X-ray crystal
                      structures of wild-type HpMTAN cocrystallized with
                      S-adenosylhomocysteine (SAH), Formycin A (FMA), and
                      (3R,4S)-4-(4-Chlorophenylthiomethyl)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxypyrrolidine
                      (p-ClPh-Thio-DADMe-ImmA) as well as one neutron/X-ray
                      crystal structure of an inactive variant (HpMTAN-D198N)
                      cocrystallized with SAH. These results support a mechanism
                      of D198 pKa elevation through the unexpected sharing of a
                      proton with atom N7 of the adenine moiety possessing
                      unconventional hydrogen-bond geometry. Additionally, the
                      neutron structures also highlight active site features that
                      promote the stabilization of the transition state and slight
                      variations in these interactions that result in 100-fold
                      difference in binding affinities between the DADMe-ImmA and
                      ImmA analogs.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {000},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
                      Neutron Research (JCNS) (POF3-623) / 6215 - Soft Matter,
                      Health and Life Sciences (POF3-621)},
      pid          = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6G4 /
                      G:(DE-HGF)POF3-6215},
      experiment   = {EXP:(DE-MLZ)BIODIFF-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000388835700068},
      pubmed       = {pmid:27856757},
      doi          = {10.1073/pnas.1609718113},
      url          = {https://juser.fz-juelich.de/record/826421},
}