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@ARTICLE{Dmitrieva:1024692,
      author       = {Dmitrieva, Nataliia 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},
      journal      = {bioRxiv beta},
      address      = {Cold Spring Harbor},
      publisher    = {Cold Spring Harbor Laboratory, NY},
      reportid     = {FZJ-2024-02365},
      year         = {2024},
      note         = {Preprint publicly available},
      abstract     = {The solute carrier 17 (SLC17) family contains anion
                      transporters that accumulate neurotransmitters in secretory
                      vesicles, remove carboxylated monosaccharides from
                      lysosomes, or extrude organic anions from the kidneys and
                      the liver. We combined experimental and computational
                      approaches to describe the transport mechanisms of a model
                      bacterial protein, the D-galactonate transporter DgoT, at
                      atomic resolution. We found that protonation of D46 and E133
                      precedes galacto-nate binding and that substrate binding
                      induces closure of the extracellular gate, with the
                      conserved R47 coupling substrate binding to transmembrane
                      helix movement. After isomerization to an inward-facing
                      conformation, deprotonation of E133 and subsequent proton
                      transfer from D46 to E133 opens the intracellular gate and
                      permits galactonate dissociation. After release of the
                      second proton, apo DgoT returns to the outward-facing
                      conformation. Our results provide a framework to understand
                      how various SLC17 transport functions with distinct
                      transport stoichiometries can be attained through subtle
                      variations in proton and substrate binding/unbinding.},
      cin          = {IBI-1 / IAS-5 / INM-9},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBI-1-20200312 / I:(DE-Juel1)IAS-5-20120330 /
                      I:(DE-Juel1)INM-9-20140121},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524) / 5252 - Brain Dysfunction and Plasticity
                      (POF4-525) / DFG project 291198853 - FOR 2518: Funktionale
                      Dynamik von Ionenkanälen und Transportern - DynIon -
                      (291198853) / DFG project 329460521 - Protonentransfer und
                      Substraterkennung in SLC17-Transportern (329460521)},
      pid          = {G:(DE-HGF)POF4-5241 / G:(DE-HGF)POF4-5252 /
                      G:(GEPRIS)291198853 / G:(GEPRIS)329460521},
      typ          = {PUB:(DE-HGF)25},
      doi          = {10.1101/2024.02.07.579339},
      url          = {https://juser.fz-juelich.de/record/1024692},
}