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@ARTICLE{Fahlke:885449,
      author       = {Fahlke, Christoph and Balandin, Taras and Astashkin, Roman
                      and Alleva, Claudia and Machtens, Jan-Philipp and Gordeliy,
                      Valentin and Baeken, Christian and Kovalev, Kirill and
                      Berndt, Meike},
      title        = {{N}a + -dependent gate dynamics and electrostatic
                      attraction ensure substrate coupling in glutamate
                      transporters},
      journal      = {Science advances},
      volume       = {6},
      number       = {47},
      issn         = {2375-2548},
      address      = {Washington, DC [u.a.]},
      publisher    = {Assoc.},
      reportid     = {FZJ-2020-03832},
      pages        = {eaba9854 -},
      year         = {2020},
      abstract     = {Excitatory amino acid transporters (EAATs) harness [Na+],
                      [K+], and [H+] gradients for fast and efficient glutamate
                      removal from the synaptic cleft. Since each glutamate is
                      cotransported with three Na+ ions, [Na+] gradients are the
                      predominant driving force for glutamate uptake. We combined
                      all-atom molecular dynamics simulations, fluorescence
                      spectroscopy, and x-ray crystallography to study
                      Na+:substrate coupling in the EAAT homolog GltPh. A lipidic
                      cubic phase x-ray crystal structure of wild-type, Na+-only
                      bound GltPh at 2.5-Å resolution revealed the fully open,
                      outward-facing state primed for subsequent substrate
                      binding. Simulations and kinetic experiments established
                      that only the binding of two Na+ ions to the Na1 and Na3
                      sites ensures complete HP2 gate opening via a conformational
                      selection-like mechanism and enables high-affinity substrate
                      binding via electrostatic attraction. The combination of
                      Na+-stabilized gate opening and electrostatic coupling of
                      aspartate to Na+ binding provides a constant Na+:substrate
                      transport stoichiometry over a broad range of
                      neurotransmitter concentrations.},
      cin          = {IBI-1 / IBI-7 / JARA-HPC},
      ddc          = {500},
      cid          = {I:(DE-Juel1)IBI-1-20200312 / I:(DE-Juel1)IBI-7-20200312 /
                      $I:(DE-82)080012_20140620$},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551) /
                      MOLECULAR MODELLING OF BIFUNCTIONAL MEMBRANE TRANSPORT
                      PROTEINS $(jics40_20190501)$ / Molecular dynamics
                      simulations of P2X receptors $(jara0180_20200501)$ /
                      Multiscale simulations of voltage-gated sodium channel
                      complexes and clusters $(jics42_20191101)$ / Molecular
                      dynamics of the SLC26 family of ion channels and
                      transporters $(jara0177_20191101)$},
      pid          = {G:(DE-HGF)POF3-551 / $G:(DE-Juel1)jics40_20190501$ /
                      $G:(DE-Juel1)jara0180_20200501$ /
                      $G:(DE-Juel1)jics42_20191101$ /
                      $G:(DE-Juel1)jara0177_20191101$},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:33208356},
      UT           = {WOS:000592173500003},
      doi          = {10.1126/sciadv.aba9854},
      url          = {https://juser.fz-juelich.de/record/885449},
}