4izm | pdb_00004izm

Crystal structure of GltPh L66C-S300C mutant crosslinked with divalent mercury

spinqualitylabelsall models 4izm, resolution 4.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4izm is a 3 chain structure with sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ASP, HG, NA Related: 2nwl, 2nww, 3v8f, 3v8g, 3kbc, 2nwx Gene: PH1295 (Pyrococcus horikoshii) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Glutamate transporters catalyze concentrative uptake of the neurotransmitter into glial cells and neurons. Their transport cycle involves binding and release of the substrate on the extra- and intracellular sides of the plasma membranes and translocation of the substrate-binding site across the lipid bilayers. The energy of the ionic gradients, mainly sodium, fuels the cycle. Here, we used a cross-linking approach to trap a glutamate transporter homolog from Pyrococcus horikoshii in key conformational states with the substrate-binding site facing either the extracellular or the intracellular side of the membrane to study binding thermodynamics. We show that the chemical potential of sodium ions in solution is exclusively coupled to substrate binding and release, not to substrate translocation. Despite the transporter's structural symmetry, the binding mechanisms are distinct on the opposite sides of the membrane and more complex than the current models suggest. Binding thermodynamics of a glutamate transporter homolog.,Reyes N, Oh S, Boudker O Nat Struct Mol Biol. 2013 May;20(5):634-40. doi: 10.1038/nsmb.2548. Epub 2013 Apr, 7. PMID:23563139 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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