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@ARTICLE{Fruergaard:486058,
      author       = {Fruergaard, Marlene U. and Dach, Ingrid and Andersen, Jacob
                      L. and Ozol, Mette and Shahsavar, Azadeh and Quistgaard,
                      Esben M. and Poulsen, Hanne and Fedosova, Natalya U. and
                      Nissen, Poul},
      title        = {{T}he {N}a$^+$,{K}$^+$-{ATP}ase in complex with beryllium
                      fluoride mimics an {ATP}ase phosphorylated state},
      journal      = {The journal of biological chemistry},
      volume       = {298},
      number       = {9},
      issn         = {0021-9258},
      address      = {Bethesda, MD.},
      publisher    = {American Soc. for Biochemistry and Molecular Biology},
      reportid     = {PUBDB-2022-07058},
      pages        = {102317},
      year         = {2022},
      note         = {ISSN 0021-9258 not unique: **2 hits**.},
      abstract     = {The Na$^+$,K$^+$-ATPase generates electrochemical gradients
                      of Na$^+$ and K$^+$ across the plasma membrane via a
                      functional cycle that includes various phosphoenzyme
                      intermediates. However, the structure and function of these
                      intermediates and how metal fluorides mimick them require
                      further investigation. Here, we describe a 4.0 Å resolution
                      crystal structure and functional properties of the pig
                      kidney Na$^+$,K$^+$-ATPase stabilized by the inhibitor
                      beryllium fluoride (denoted E2–BeF$_x$). E2–BeF$_x$ is
                      expected to mimic properties of the E2P phosphoenzyme, yet
                      with unknown characteristics of ion and ligand binding. The
                      structure resembles the E2P form obtained by phosphorylation
                      from inorganic phosphate (P$_i$) and stabilized by
                      cardiotonic steroids, including a low-affinity Mg$^{2+}$
                      site near ion binding site II. Our anomalous Fourier
                      analysis of the crystals soaked in Rb$^+$ (a K$^+$ congener)
                      followed by a low-resolution rigid-body refinement
                      (6.9–7.5 Å) revealed preocclusion transitions leading to
                      activation of the dephosphorylation reaction. We show that
                      the Mg$^{2+}$ location indicates a site of initial K$^+$
                      recognition and acceptance upon binding to the outward-open
                      E2P state after Na$^+$ release. Furthermore, using binding
                      and activity studies, we find that the BeF$_x$-inhibited
                      enzyme is also able to bind ADP/ATP and Na$^+$. These
                      results relate the E2–BeF$_x$ complex to a transient
                      K$^+$- and ADP-sensitive E∗P intermediate of the
                      functional cycle of the Na$^+$,K$^+$-ATPase, prior to E2P.},
      cin          = {EMBL-User},
      ddc          = {610},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P14-20150101 / EXP:(DE-H253)P-P13-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:35926706},
      UT           = {WOS:000863323200005},
      doi          = {10.1016/j.jbc.2022.102317},
      url          = {https://bib-pubdb1.desy.de/record/486058},
}