View source for 3f3e


==Crystal structure of LeuT bound to L-leucine (30 mM) and sodium==
<StructureSection load='3f3e' size='340' side='right'caption='[[3f3e]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3f3e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. The March 2014 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Neurotransmitter Transporters''  by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2014_3 10.2210/rcsb_pdb/mom_2014_3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F3E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3F3E FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2a65|2a65]], [[2qei|2qei]], [[3f3a|3f3a]], [[3f3c|3f3c]], [[3f3d|3f3d]], [[3f48|3f48]], [[3f4i|3f4i]], [[3f4j|3f4j]]</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" Huber and Stetter 2001])</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=3f3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f3e OCA], [http://pdbe.org/3f3e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3f3e RCSB], [http://www.ebi.ac.uk/pdbsum/3f3e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3f3e ProSAT]</span></td></tr>
</table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f3/3f3e_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3f3e ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Secondary transporters are workhorses of cellular membranes, catalyzing the movement of small molecules and ions across the bilayer and coupling substrate passage to ion gradients. However, the conformational changes that accompany substrate transport, the mechanism by which a substrate moves through the transporter, and principles of competitive inhibition remain unclear. We used crystallographic and functional studies on the leucine transporter (LeuT), a model for neurotransmitter sodium symporters, to show that various amino acid substrates induce the same occluded conformational state and that a competitive inhibitor, tryptophan (Trp), traps LeuT in an open-to-out conformation. In the Trp complex, the extracellular gate residues arginine 30 and aspartic acid 404 define a second weak binding site for substrates or inhibitors as they permeate from the extracellular solution to the primary substrate site, which demonstrates how residues that participate in gating also mediate permeation.

A competitive inhibitor traps LeuT in an open-to-out conformation.,Singh SK, Piscitelli CL, Yamashita A, Gouaux E Science. 2008 Dec 12;322(5908):1655-61. PMID:19074341<ref>PMID:19074341</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3f3e" style="background-color:#fffaf0;"></div>

==See Also==
*[[Leucine transporter|Leucine transporter]]
*[[Symporter|Symporter]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aquifex aeolicus huber and stetter 2001]]
[[Category: Large Structures]]
[[Category: Neurotransmitter Transporters]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Gouaux, E]]
[[Category: Piscitelli, C L]]
[[Category: Singh, S K]]
[[Category: Yamashita, A]]
[[Category: Nss]]
[[Category: Slc6]]
[[Category: Sodium-coupled]]
[[Category: Symport]]
[[Category: Transmembrane]]
[[Category: Transport]]
[[Category: Transport protein]]
[[Category: Transporter]]