7dj2: Difference between revisions
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==Crystal structure of the G26C/E290S mutant of LeuT== | |||
<StructureSection load='7dj2' size='340' side='right'caption='[[7dj2]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7dj2]] 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=7DJ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DJ2 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]] 2.4Å</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>, <scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=7dj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dj2 OCA], [https://pdbe.org/7dj2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dj2 RCSB], [https://www.ebi.ac.uk/pdbsum/7dj2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dj2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/O67854_AQUAE O67854_AQUAE] | |||
<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> | ||
[[Category: | <div class="pdbe-citations 7dj2" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Fan | ==See Also== | ||
[[Category: Sun | *[[Symporter 3D structures|Symporter 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aquifex aeolicus]] | |||
[[Category: Large Structures]] | |||
[[Category: Fan J]] | |||
[[Category: Sun Z]] | |||
[[Category: Xiao Y]] | |||
[[Category: Zhou X]] | |||
Latest revision as of 19:34, 29 November 2023
Crystal structure of the G26C/E290S mutant of LeuTCrystal structure of the G26C/E290S mutant of LeuT
Structural highlights
FunctionPublication 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. See AlsoReferences
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