5e9s

Crystal structure of substrate-bound glutamate transporter homologue GltTk

spinqualitylabelsall models 5e9s, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5e9s is a 3 chain structure with sequence from Thermococcus kodakarensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: 1PE, ASP, DMU, NA, P6G, PEG, PGE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5JID0_THEKO Publication Abstract from PubMed 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 GltTk 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. Coupled binding mechanism of three sodium ions and aspartate in the glutamate transporter homologue GltTk.,Guskov A, Jensen S, Faustino I, Marrink SJ, Slotboom DJ Nat Commun. 2016 Nov 10;7:13420. doi: 10.1038/ncomms13420. PMID:27830699 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Symporter 3D structures

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