Hauptseite > Publikationsdatenbank > Na + -dependent gate dynamics and electrostatic attraction ensure substrate coupling in glutamate transporters > print

001     885449
005     20220930130254.0
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100 1 _ |a Fahlke, Christoph
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245 _ _ |a Na + -dependent gate dynamics and electrostatic attraction ensure substrate coupling in glutamate transporters
260 _ _ |a Washington, DC [u.a.]
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520 _ _ |a 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.
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536 _ _ |a Molecular dynamics simulations of P2X receptors (jara0180_20200501)
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536 _ _ |a Multiscale simulations of voltage-gated sodium channel complexes and clusters (jics42_20191101)
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536 _ _ |a Molecular dynamics of the SLC26 family of ion channels and transporters (jara0177_20191101)
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700 1 _ |a Alleva, Claudia
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700 1 _ |a Machtens, Jan-Philipp
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700 1 _ |a Gordeliy, Valentin
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700 1 _ |a Baeken, Christian
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700 1 _ |a Kovalev, Kirill
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773 _ _ |a 10.1126/sciadv.aba9854
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