Publication

Binding and transport of D-aspartate by the glutamate transporter homologue GltTk

Arkhipova, V. I., Trinco, G., Thijs, E., Jensen, S., Slotboom, D. & Guskov, A., 1-May-2019, In : eLife. 8, e45286.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Arkhipova, V. I., Trinco, G., Thijs, E., Jensen, S., Slotboom, D., & Guskov, A. (2019). Binding and transport of D-aspartate by the glutamate transporter homologue GltTk. eLife, 8, [e45286]. https://doi.org/10.7554/eLife.45286

Author

Arkhipova, Valentina Ivanovna ; Trinco, Gianluca ; Thijs, Ettema ; Jensen, Sonja ; Slotboom, Dirk ; Guskov, Albert. / Binding and transport of D-aspartate by the glutamate transporter homologue GltTk. In: eLife. 2019 ; Vol. 8.

Harvard

Arkhipova, VI, Trinco, G, Thijs, E, Jensen, S, Slotboom, D & Guskov, A 2019, 'Binding and transport of D-aspartate by the glutamate transporter homologue GltTk' eLife, vol. 8, e45286. https://doi.org/10.7554/eLife.45286

Standard

Binding and transport of D-aspartate by the glutamate transporter homologue GltTk. / Arkhipova, Valentina Ivanovna; Trinco, Gianluca; Thijs, Ettema; Jensen, Sonja; Slotboom, Dirk; Guskov, Albert.

In: eLife, Vol. 8, e45286, 01.05.2019.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Arkhipova VI, Trinco G, Thijs E, Jensen S, Slotboom D, Guskov A. Binding and transport of D-aspartate by the glutamate transporter homologue GltTk. eLife. 2019 May 1;8. e45286. https://doi.org/10.7554/eLife.45286


BibTeX

@article{bc24c0446b9a482caaf0f63fbb6da794,
title = "Binding and transport of D-aspartate by the glutamate transporter homologue GltTk",
abstract = "Mammalian glutamate transporters are crucial players in neuronal communication as they perform neurotransmitter reuptake from the synaptic cleft. Besides L-glutamate and L-aspartate, they also recognize D-aspartate, which might participate in mammalian neurotransmission and/or neuromodulation. Much of the mechanistic insight in glutamate transport comes from studies of the archaeal homologues GltPh from Pyrococcus horikoshii and GltTk from Thermococcus kodakarensis. Here, we show that GltTk transports D-aspartate with identical Na+ : substrate coupling stoichiometry as L-aspartate, and that the affinities (Kd and Km) for the two substrates are similar. We determined a crystal structure of GltTk with bound D-aspartate at 2.8 {\AA} resolution. Comparison of the L- and D-aspartate bound GltTk structures revealed that D-aspartate is accommodated with only minor rearrangements in the structure of the binding site. The structure explains how the geometrically different molecules L- and D-aspartate are recognized and transported by the protein in the same way.",
author = "Arkhipova, {Valentina Ivanovna} and Gianluca Trinco and Ettema Thijs and Sonja Jensen and Dirk Slotboom and Albert Guskov",
year = "2019",
month = "5",
day = "1",
doi = "10.7554/eLife.45286",
language = "English",
volume = "8",
journal = "eLife",
issn = "2050-084X",
publisher = "ELIFE SCIENCES PUBLICATIONS LTD",

}

RIS

TY - JOUR

T1 - Binding and transport of D-aspartate by the glutamate transporter homologue GltTk

AU - Arkhipova, Valentina Ivanovna

AU - Trinco, Gianluca

AU - Thijs, Ettema

AU - Jensen, Sonja

AU - Slotboom, Dirk

AU - Guskov, Albert

PY - 2019/5/1

Y1 - 2019/5/1

N2 - Mammalian glutamate transporters are crucial players in neuronal communication as they perform neurotransmitter reuptake from the synaptic cleft. Besides L-glutamate and L-aspartate, they also recognize D-aspartate, which might participate in mammalian neurotransmission and/or neuromodulation. Much of the mechanistic insight in glutamate transport comes from studies of the archaeal homologues GltPh from Pyrococcus horikoshii and GltTk from Thermococcus kodakarensis. Here, we show that GltTk transports D-aspartate with identical Na+ : substrate coupling stoichiometry as L-aspartate, and that the affinities (Kd and Km) for the two substrates are similar. We determined a crystal structure of GltTk with bound D-aspartate at 2.8 Å resolution. Comparison of the L- and D-aspartate bound GltTk structures revealed that D-aspartate is accommodated with only minor rearrangements in the structure of the binding site. The structure explains how the geometrically different molecules L- and D-aspartate are recognized and transported by the protein in the same way.

AB - Mammalian glutamate transporters are crucial players in neuronal communication as they perform neurotransmitter reuptake from the synaptic cleft. Besides L-glutamate and L-aspartate, they also recognize D-aspartate, which might participate in mammalian neurotransmission and/or neuromodulation. Much of the mechanistic insight in glutamate transport comes from studies of the archaeal homologues GltPh from Pyrococcus horikoshii and GltTk from Thermococcus kodakarensis. Here, we show that GltTk transports D-aspartate with identical Na+ : substrate coupling stoichiometry as L-aspartate, and that the affinities (Kd and Km) for the two substrates are similar. We determined a crystal structure of GltTk with bound D-aspartate at 2.8 Å resolution. Comparison of the L- and D-aspartate bound GltTk structures revealed that D-aspartate is accommodated with only minor rearrangements in the structure of the binding site. The structure explains how the geometrically different molecules L- and D-aspartate are recognized and transported by the protein in the same way.

U2 - 10.7554/eLife.45286

DO - 10.7554/eLife.45286

M3 - Article

VL - 8

JO - eLife

JF - eLife

SN - 2050-084X

M1 - e45286

ER -

ID: 79516241