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==Crystal structure of LeuT bound to L-leucine in space group P21 from lipid bicelles==
==Crystal structure of LeuT bound to L-leucine in space group P21 from lipid bicelles==
<StructureSection load='3usj' size='340' side='right' caption='[[3usj]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
<StructureSection load='3usj' size='340' side='right'caption='[[3usj]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3usj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3USJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3USJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[3usj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3USJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3USJ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</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]] 3.5&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3usg|3usg]], [[3usi|3usi]], [[3usk|3usk]], [[3usl|3usl]], [[3usm|3usm]], [[3uso|3uso]], [[3usp|3usp]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</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=63363 Aquifex aeolicus])</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=3usj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3usj OCA], [https://pdbe.org/3usj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3usj RCSB], [https://www.ebi.ac.uk/pdbsum/3usj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3usj 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=3usj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3usj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3usj RCSB], [http://www.ebi.ac.uk/pdbsum/3usj PDBsum]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/O67854_AQUAE O67854_AQUAE]
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<ref>PMID:22245965</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==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: Aquifex aeolicus]]
[[Category: Aquifex aeolicus]]
[[Category: Elferich, J]]
[[Category: Large Structures]]
[[Category: Gouaux, E]]
[[Category: Elferich J]]
[[Category: Wang, H]]
[[Category: Gouaux E]]
[[Category: Leucine transporter]]
[[Category: Wang H]]
[[Category: Transport protein]]

Latest revision as of 13:27, 1 March 2024

Crystal structure of LeuT bound to L-leucine in space group P21 from lipid bicellesCrystal structure of LeuT bound to L-leucine in space group P21 from lipid bicelles

Structural highlights

3usj 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 3.5Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

O67854_AQUAE

See Also

3usj, resolution 3.50Å

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