6R7R

Crystal structure of the glutamate transporter homologue GltTk in complex with D-aspartate

Summary for 6R7R

• Entry DOI: 10.2210/pdb6r7r/pdb
• Related: 5E9S
• Descriptor: Proton/glutamate symporter, SDF family, SODIUM ION, D-ASPARTIC ACID, ... (9 entities in total)
• Functional Keywords: amino acid transporter, aspartate transport, glutamate transporter homologue, transport protein, membrane protein
• Biological source: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
• Total number of polymer chains: 3
• Total formula weight: 143865.99

Authors

Arkhipova, V.,Guskov, A.,Slotboom, D.J. (deposition date: 2019-03-29, release date: 2019-04-17, Last modification date: 2024-01-24)

Primary citation

Arkhipova, V.,Trinco, G.,Ettema, T.W.,Jensen, S.,Slotboom, D.J.,Guskov, A.
Binding and transport of D-aspartate by the glutamate transporter homolog Glt Tk .
Elife, 8:-, 2019

PubMed 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 archeal homologs Glt from and Glt from . Here, we show that Glt transports D-aspartate with identical Na: substrate coupling stoichiometry as L-aspartate, and that the affinities ( and ) for the two substrates are similar. We determined a crystal structure of Glt with bound D-aspartate at 2.8 Å resolution. Comparison of the L- and D-aspartate bound Glt 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.

PubMed: 30969168
DOI: 10.7554/eLife.45286

Experimental method

X-RAY DIFFRACTION (2.8 Å)