% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Dmitrieva:1032107,
      author       = {Dmitrieva, Natalia and Gholami, Samira and Alleva, Claudia
                      and Carloni, Paolo and Alfonso-Prieto, Mercedes and Fahlke,
                      Christoph},
      title        = {{T}ransport mechanism of {D}go{T}, a bacterial homolog of
                      {SLC}17 organic anion transporters},
      address      = {Hoboken, NJ [u.a.]},
      publisher    = {Wiley},
      reportid     = {FZJ-2024-06005},
      year         = {2024},
      note         = {We thank Drs Andre Bazzone, Bassam Haddad, Andrei
                      Kostritskii, PiersilvioLongo and Jan-Philipp Machtens for
                      helpful discussions and Meike Berndt forexcellent technical
                      support. This work was supported by the
                      DeutscheForschungsgemeinschaft (German Research Foundation)
                      to ChF (FA 301/15–2), PC (CA 973/27-2) and MAP (AL
                      2511/1-2) as part of Research Unit FOR2518, DynIon. The
                      authors gratefully acknowledge computing time on the
                      supercomputer JURECA at Forschungszentrum Jülich under
                      grants dgoth and vglut-pt.Open Access article as part of the
                      DEAL agreement with Wiley.},
      abstract     = {The solute carrier 17 (SLC17) family contains anion
                      transportersthat accumulate neurotransmitters in secretory
                      vesicles, removecarboxylated monosaccharides from lysosomes,
                      or extrude organicanions from the kidneys and liver.We
                      combined classical moleculardynamics simulations, Markov
                      state modeling and hybrid firstprinciples quantum
                      mechanical/classical mechanical (QM/MM)simulations with
                      experimental approaches to describe the transportmechanisms
                      of a model bacterial protein, the D-galactonatetransporter
                      DgoT, at atomic resolution. We found that protonationof D46
                      and E133 precedes galactonate binding and that
                      substratebinding induces closure of the extracellular gate,
                      with the conservedR47 coupling substrate binding to
                      transmembrane helixmovement. After isomerization to an
                      inward-facing conformation,deprotonation of E133 and
                      subsequent proton transfer from D46 toE133 opens the
                      intracellular gate and permits galactonate
                      dissociationeither in its unprotonated form or after proton
                      transferfrom E133. After release of the second proton, apo
                      DgoT returns tothe outward-facing conformation. Our results
                      provide a frameworkto understand how various SLC17 transport
                      functions with distincttransport stoichiometries can be
                      attained through subtle variationsin proton and substrate
                      binding/unbinding.},
      cin          = {IBI-1 / INM-9},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBI-1-20200312 / I:(DE-Juel1)INM-9-20140121},
      pnm          = {5243 - Information Processing in Distributed Systems
                      (POF4-524) / 5241 - Molecular Information Processing in
                      Cellular Systems (POF4-524) / DFG project
                      G:(GEPRIS)426950122 - FOR 5046: Integrative Analyse
                      epithelialer SLC26 Anionentransporter – von der
                      molekularen Struktur zur Pathophysiologie (426950122) / DFG
                      project G:(GEPRIS)291198853 - FOR 2518: Funktionale Dynamik
                      von Ionenkanälen und Transportern - DynIon - (291198853) /
                      DFG project G:(GEPRIS)329460521 - Protonentransfer und
                      Substraterkennung in SLC17-Transportern (329460521)},
      pid          = {G:(DE-HGF)POF4-5243 / G:(DE-HGF)POF4-5241 /
                      G:(GEPRIS)426950122 / G:(GEPRIS)291198853 /
                      G:(GEPRIS)329460521},
      typ          = {PUB:(DE-HGF)25},
      url          = {https://juser.fz-juelich.de/record/1032107},
}