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4fy0

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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==
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<StructureSection load='4fy0' size='340' side='right' caption='[[4fy0]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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<StructureSection load='4fy0' size='340' side='right'caption='[[4fy0]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fxz|4fxz]]</td></tr>
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<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>
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<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>
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<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>
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<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>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/O67854_AQUAE O67854_AQUAE]
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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<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]]
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== References ==
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*[[Symporter 3D structures|Symporter 3D structures]]
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aquae]]
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[[Category: Aquifex aeolicus VF5]]
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[[Category: Gouaux, E]]
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[[Category: Large Structures]]
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[[Category: Wang, H]]
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[[Category: Gouaux E]]
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[[Category: Amino acid transporter]]
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[[Category: Wang H]]
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[[Category: Transport protein]]
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Current revision

Crystal structure of LeuT-F253A bound to L-selenomethionine from lipid bicelles

PDB ID 4fy0

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