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5DWY

Crystal structure of a substrate-free glutamate transporter homologue GltTk

Summary for 5DWY
Entry DOI10.2210/pdb5dwy/pdb
Related4KY0
DescriptorProton/glutamate symporter, SDF family, TRIETHYLENE GLYCOL, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
Functional Keywordsamino acid transporter, aspartate transport, glutamate transport homologue, transport protein, membrane protein
Biological sourceThermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
Total number of polymer chains3
Total formula weight144733.49
Authors
Guskov, A.,Slotboom, D.J. (deposition date: 2015-09-23, release date: 2016-09-28, Last modification date: 2024-01-10)
Primary citationGuskov, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

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