View source for 5jae


==LeuT in the outward-oriented, Na+-free return state, P21 form at pH 6.5==
<StructureSection load='5jae' size='340' side='right'caption='[[5jae]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5jae]] is a 2 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=5JAE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JAE FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene></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=5jae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jae OCA], [https://pdbe.org/5jae PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jae RCSB], [https://www.ebi.ac.uk/pdbsum/5jae PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jae ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O67854_AQUAE O67854_AQUAE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial members of the neurotransmitter:sodium symporter (NSS) family perform Na(+)-dependent amino-acid uptake and extrude H(+) in return. Previous NSS structures represent intermediates of Na(+)/substrate binding or intracellular release, but not the inward-to-outward return transition. Here we report crystal structures of Aquifex aeolicus LeuT in an outward-oriented, Na(+)- and substrate-free state likely to be H(+)-occluded. We find a remarkable rotation of the conserved Leu25 into the empty substrate-binding pocket and rearrangements of the empty Na(+) sites. Mutational studies of the equivalent Leu99 in the human serotonin transporter show a critical role of this residue on the transport rate. Molecular dynamics simulations show that extracellular Na(+) is blocked unless Leu25 is rotated out of the substrate-binding pocket. We propose that Leu25 facilitates the inward-to-outward transition by compensating a Na(+)- and substrate-free state and acts as the gatekeeper for Na(+) binding that prevents leak in inward-outward return transitions.

A conserved leucine occupies the empty substrate site of LeuT in the Na(+)-free return state.,Malinauskaite L, Said S, Sahin C, Grouleff J, Shahsavar A, Bjerregaard H, Noer P, Severinsen K, Boesen T, Schiott B, Sinning S, Nissen P Nat Commun. 2016 May 25;7:11673. doi: 10.1038/ncomms11673. PMID:27221344<ref>PMID:27221344</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5jae" style="background-color:#fffaf0;"></div>

==See Also==
*[[Symporter 3D structures|Symporter 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aquifex aeolicus VF5]]
[[Category: Large Structures]]
[[Category: Bjerregaard H]]
[[Category: Boesen T]]
[[Category: Grouleff J]]
[[Category: Malinauskaite L]]
[[Category: Nissen P]]
[[Category: Noer P]]
[[Category: Sahin C]]
[[Category: Said S]]
[[Category: Schiott B]]
[[Category: Severinsen K]]
[[Category: Shahsavar A]]
[[Category: Sinning S]]