3uso | pdb_00003uso

Crystal structure of LeuT bound to L-selenomethionine in space group P21212 from lipid bicelles

spinqualitylabelsall models 3uso, resolution 4.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3uso is a 2 chain structure with sequence from Aquifex aeolicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 4.5Å Ligands: MSE, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O67854_AQUAE Publication Abstract from PubMed Neurotransmitter sodium symporters (NSSs) catalyze the uptake of neurotransmitters into cells, terminating neurotransmission at chemical synapses. Consistent with the role of NSSs in the central nervous system, they are implicated in multiple diseases and disorders. LeuT, from Aquifex aeolicus, is a prokaryotic ortholog of the NSS family and has contributed to our understanding of the structure, mechanism and pharmacology of NSSs. At present, however, the functional state of LeuT in crystals grown in the presence of n-octyl-beta-D-glucopyranoside (beta-OG) and the number of substrate binding sites are controversial issues. Here we present crystal structures of LeuT grown in DMPC-CHAPSO bicelles and demonstrate that the conformations of LeuT-substrate complexes in lipid bicelles and in beta-OG detergent micelles are nearly identical. Furthermore, using crystals grown in bicelles and the substrate leucine or the substrate analog selenomethionine, we find only a single substrate molecule in the primary binding site. Structures of LeuT in bicelles define conformation and substrate binding in a membrane-like context.,Wang H, Elferich J, Gouaux E Nat Struct Mol Biol. 2012 Jan 15;19(2):212-9. doi: 10.1038/nsmb.2215. PMID:22245965 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Leucine transporter Symporter 3D structures

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