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| | ==Crystal structure of LeuT-F253A bound to L-selenomethionine from lipid bicelles== | | ==Crystal structure of LeuT-F253A bound to L-selenomethionine from lipid bicelles== |
| - | <StructureSection load='4fy0' size='340' side='right' caption='[[4fy0]], [[Resolution|resolution]] 3.00Å' scene=''> | + | <StructureSection load='4fy0' size='340' side='right'caption='[[4fy0]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4fy0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquae Aquae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FY0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FY0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4fy0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FY0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FY0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fxz|4fxz]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">snf, aq_2077 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224324 AQUAE])</td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fy0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fy0 OCA], [https://pdbe.org/4fy0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fy0 RCSB], [https://www.ebi.ac.uk/pdbsum/4fy0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fy0 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fy0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fy0 OCA], [http://pdbe.org/4fy0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fy0 RCSB], [http://www.ebi.ac.uk/pdbsum/4fy0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fy0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/O67854_AQUAE O67854_AQUAE] |
| - | 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.
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| - | Substrate binds in the S1 site of the F253A mutant of LeuT, a neurotransmitter sodium symporter homologue.,Wang H, Gouaux E EMBO Rep. 2012 Jul 27. doi: 10.1038/embor.2012.110. PMID:22836580<ref>PMID:22836580</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
| + | |
| - | <div class="pdbe-citations 4fy0" style="background-color:#fffaf0;"></div>
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| | | | |
| | ==See Also== | | ==See Also== |
| | *[[Leucine transporter|Leucine transporter]] | | *[[Leucine transporter|Leucine transporter]] |
| - | == References ==
| + | *[[Symporter 3D structures|Symporter 3D structures]] |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aquae]] | + | [[Category: Aquifex aeolicus VF5]] |
| - | [[Category: Gouaux, E]] | + | [[Category: Large Structures]] |
| - | [[Category: Wang, H]] | + | [[Category: Gouaux E]] |
| - | [[Category: Amino acid transporter]] | + | [[Category: Wang H]] |
| - | [[Category: Transport protein]]
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