7dix: Difference between revisions
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==Crystal structure of LeuT in lipidic cubic phase at pH 5== | ==Crystal structure of LeuT in lipidic cubic phase at pH 5== | ||
<StructureSection load='7dix' size='340' side='right'caption='[[7dix]]' scene=''> | <StructureSection load='7dix' size='340' side='right'caption='[[7dix]], [[Resolution|resolution]] 3.49Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DIX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DIX FirstGlance]. <br> | <table><tr><td colspan='2'>[[7dix]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DIX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DIX FirstGlance]. <br> | ||
</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=7dix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dix OCA], [https://pdbe.org/7dix PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dix RCSB], [https://www.ebi.ac.uk/pdbsum/7dix PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dix ProSAT]</span></td></tr> | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7dii|7dii]], [[7dj1|7dj1]], [[7dj2|7dj2]], [[7djc|7djc]]</div></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=7dix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dix OCA], [https://pdbe.org/7dix PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dix RCSB], [https://www.ebi.ac.uk/pdbsum/7dix PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dix ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The neurotransmitter:sodium symporter (NSS) homolog LeuT from Aquifex aeolicus has proven to be a valuable model for studying the transport mechanism of the NSS family. Crystal structures have captured LeuT in key conformations visited during the transport cycle, allowing for the construction of a nearly complete model of transport, with much of the conformational dynamics studied by computational simulations. Here, we report crystal structures of LeuT representing new intermediate conformations between the outward-facing open and occluded states. These structures, combined with binding and accessibility studies, reveal details of conformational dynamics that can follow substrate binding at the central substrate-binding site (S1) of LeuT in outward-facing states, suggesting a potential competition for direction between the outward-open and outward-occluded states at this stage during substrate transport. Our structures further support an intimate interplay between the protonation state of Glu290 and binding of Na1 that may ultimately regulate the outward-open-to-occluded transition. | |||
Crystal structures of LeuT reveal conformational dynamics in the outward-facing states.,Fan J, Xiao Y, Quick M, Yang Y, Sun Z, Javitch JA, Zhou X J Biol Chem. 2021 Apr 1:100609. doi: 10.1016/j.jbc.2021.100609. PMID:33811858<ref>PMID:33811858</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7dix" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Aquifex aeolicus huber and stetter 2001]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Fan J]] | [[Category: Fan, J]] | ||
[[Category: Sun Z]] | [[Category: Sun, Z]] | ||
[[Category: Xiao Y]] | [[Category: Xiao, Y]] | ||
[[Category: Zhou X]] | [[Category: Zhou, X]] | ||
[[Category: Neurotransmitter transporter]] | |||
[[Category: Nss]] | |||
[[Category: Slc6]] | |||
[[Category: Transport protein]] | |||
Revision as of 11:33, 21 April 2021
Crystal structure of LeuT in lipidic cubic phase at pH 5Crystal structure of LeuT in lipidic cubic phase at pH 5
Structural highlights
Publication Abstract from PubMedThe neurotransmitter:sodium symporter (NSS) homolog LeuT from Aquifex aeolicus has proven to be a valuable model for studying the transport mechanism of the NSS family. Crystal structures have captured LeuT in key conformations visited during the transport cycle, allowing for the construction of a nearly complete model of transport, with much of the conformational dynamics studied by computational simulations. Here, we report crystal structures of LeuT representing new intermediate conformations between the outward-facing open and occluded states. These structures, combined with binding and accessibility studies, reveal details of conformational dynamics that can follow substrate binding at the central substrate-binding site (S1) of LeuT in outward-facing states, suggesting a potential competition for direction between the outward-open and outward-occluded states at this stage during substrate transport. Our structures further support an intimate interplay between the protonation state of Glu290 and binding of Na1 that may ultimately regulate the outward-open-to-occluded transition. Crystal structures of LeuT reveal conformational dynamics in the outward-facing states.,Fan J, Xiao Y, Quick M, Yang Y, Sun Z, Javitch JA, Zhou X J Biol Chem. 2021 Apr 1:100609. doi: 10.1016/j.jbc.2021.100609. PMID:33811858[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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