4FY0
Crystal structure of LeuT-F253A bound to L-selenomethionine from lipid bicelles
Summary for 4FY0
| Entry DOI | 10.2210/pdb4fy0/pdb |
| Related | 4FXZ |
| Descriptor | Transporter, SODIUM ION, SELENOMETHIONINE (3 entities in total) |
| Functional Keywords | amino acid transporter, transport protein |
| Biological source | Aquifex aeolicus |
| Total number of polymer chains | 1 |
| Total formula weight | 57618.67 |
| Authors | Wang, H.,Gouaux, E. (deposition date: 2012-07-03, release date: 2012-08-08, Last modification date: 2024-02-28) |
| Primary citation | Wang, H.,Gouaux, E. Substrate binds in the S1 site of the F253A mutant of LeuT, a neurotransmitter sodium symporter homologue. Embo Rep., 13:861-866, 2012 Cited by PubMed Abstract: LeuT serves as the model protein for understanding the relationships between structure, mechanism and pharmacology in neurotransmitter sodium symporters (NSSs). At the present time, however, there is a vigorous debate over whether there is a single high-affinity substrate site (S1) located at the original, crystallographically determined substrate site or whether there are two high-affinity substrates sites, one at the primary or S1 site and the other at a second site (S2) located at the base of the extracellular vestibule. In an effort to address the controversy over the number of high-affinity substrate sites in LeuT, one group studied the F253A mutant of LeuT and asserted that in this mutant substrate binds exclusively to the S2 site and that 1 mM clomipramine entirely ablates substrate binding to the S2 site. Here we study the binding of substrate to the F253A mutant of LeuT using ligand binding and X-ray crystallographic methods. Both experimental methods unambiguously show that substrate binds to the S1 site of the F253A mutant and that binding is retained in the presence of 1 mM clomipramine. These studies, in combination with previous work, are consistent with a mechanism for LeuT that involves a single high-affinity substrate binding site. PubMed: 22836580DOI: 10.1038/embor.2012.110 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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