5E9S

Crystal structure of substrate-bound glutamate transporter homologue GltTk

Summary for 5E9S

• Entry DOI: 10.2210/pdb5e9s/pdb
• Related: 5DWY
• Descriptor: Proton/glutamate symporter, SDF family, ASPARTIC ACID, SODIUM ION, ... (8 entities in total)
• Functional Keywords: amino acid transporter, aspartate transport, glutamate transport homologue, transport protein, membrane protein
• Biological source: Thermococcus kodakarensis
• Total number of polymer chains: 3
• Total formula weight: 149742.77

Authors

Guskov, A.,Slotboom, D.J. (deposition date: 2015-10-15, release date: 2016-09-28, Last modification date: 2024-01-10)

Primary citation

Guskov, A.,Jensen, S.,Faustino, I.,Marrink, S.J.,Slotboom, D.J.
Coupled binding mechanism of three sodium ions and aspartate in the glutamate transporter homologue GltTk.
Nat Commun, 7:13420-13420, 2016

PubMed Abstract: Glutamate transporters catalyse the thermodynamically unfavourable transport of anionic amino acids across the cell membrane by coupling it to the downhill transport of cations. This coupling mechanism is still poorly understood, in part because the available crystal structures of these transporters are of relatively low resolution. Here we solve crystal structures of the archaeal transporter Glt in the presence and absence of aspartate and use molecular dynamics simulations and binding assays to show how strict coupling between the binding of three sodium ions and aspartate takes place.

PubMed: 27830699
DOI: 10.1038/ncomms13420

Experimental method

X-RAY DIFFRACTION (2.8 Å)