6XWP
Structure of glutamate transporter homologue GltTk in unsaturated conditions - outward-outward-inward configuration
Summary for 6XWP
| Entry DOI | 10.2210/pdb6xwp/pdb |
| Related | 6XWN 6XWO 6XWQ 6XWR |
| EMDB information | 10634 |
| Descriptor | Proton/glutamate symporter, SDF family, ASPARTIC ACID (2 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 | 137006.82 |
| Authors | Arkhipova, V.,Slotboom, D.J.,Guskov, A. (deposition date: 2020-01-24, release date: 2020-03-04, Last modification date: 2024-05-22) |
| Primary citation | Arkhipova, V.,Guskov, A.,Slotboom, D.J. Structural ensemble of a glutamate transporter homologue in lipid nanodisc environment. Nat Commun, 11:998-998, 2020 Cited by PubMed Abstract: Glutamate transporters are cation-coupled secondary active membrane transporters that clear the neurotransmitter L-glutamate from the synaptic cleft. These transporters are homotrimers, with each protomer functioning independently by an elevator-type mechanism, in which a mobile transport domain alternates between inward- and outward-oriented states. Using single-particle cryo-EM we have determined five structures of the glutamate transporter homologue Glt, a Na- L-aspartate symporter, embedded in lipid nanodiscs. Dependent on the substrate concentrations used, the protomers of the trimer adopt a variety of asymmetrical conformations, consistent with the independent movement. Six of the 15 resolved protomers are in a hitherto elusive state of the transport cycle in which the inward-facing transporters are loaded with Na ions. These structures explain how substrate-leakage is prevented - a strict requirement for coupled transport. The belt protein of the lipid nanodiscs bends around the inward oriented protomers, suggesting that membrane deformations occur during transport. PubMed: 32081874DOI: 10.1038/s41467-020-14834-8 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.38 Å) |
Structure validation
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