4KY0
Crystal structure of a substrate-free glutamate transporter homologue from Thermococcus kodakarensis
Summary for 4KY0
| Entry DOI | 10.2210/pdb4ky0/pdb |
| Descriptor | Proton/glutamate symporter, SDF family, TETRAETHYLENE GLYCOL (2 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 | 137931.95 |
| Authors | Guskov, A.,Jensen, S.,Rempel, S.,Hanelt, I.,Slotboom, D.J. (deposition date: 2013-05-28, release date: 2013-09-11, Last modification date: 2023-09-20) |
| Primary citation | Jensen, S.,Guskov, A.,Rempel, S.,Hanelt, I.,Slotboom, D.J. Crystal structure of a substrate-free aspartate transporter. Nat.Struct.Mol.Biol., 20:1224-1226, 2013 Cited by PubMed Abstract: Archaeal glutamate transporter homologs catalyze the coupled uptake of aspartate and three sodium ions. After the delivery of the substrate and sodium ions to the cytoplasm, the empty binding site must reorient to the outward-facing conformation to reset the transporter. Here, we report a crystal structure of the substrate-free transporter GltTk from Thermococcus kodakarensis, which provides insight into the mechanism of this essential step in the translocation cycle. PubMed: 24013209DOI: 10.1038/nsmb.2663 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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