6xwp: Difference between revisions
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==Structure of glutamate transporter homologue GltTk in unsaturated conditions - outward-outward-inward configuration== | |||
<StructureSection load='6xwp' size='340' side='right'caption='[[6xwp]], [[Resolution|resolution]] 3.38Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6xwp]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XWP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6XWP FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6xwo|6xwo]], [[6xwq|6xwq]], [[6xwr|6xwr]], [[6xwn|6xwn]]</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=6xwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xwp OCA], [http://pdbe.org/6xwp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6xwp RCSB], [http://www.ebi.ac.uk/pdbsum/6xwp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6xwp ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Glutamate transporters are cation-coupled secondary active membrane transporters that clear the neurotransmitter L-glutamate from the synaptic cleft. These transporters are homotrimers, with each protomer functioning independently by an elevator-type mechanism, in which a mobile transport domain alternates between inward- and outward-oriented states. Using single-particle cryo-EM we have determined five structures of the glutamate transporter homologue GltTk, a Na(+)- L-aspartate symporter, embedded in lipid nanodiscs. Dependent on the substrate concentrations used, the protomers of the trimer adopt a variety of asymmetrical conformations, consistent with the independent movement. Six of the 15 resolved protomers are in a hitherto elusive state of the transport cycle in which the inward-facing transporters are loaded with Na(+) ions. These structures explain how substrate-leakage is prevented - a strict requirement for coupled transport. The belt protein of the lipid nanodiscs bends around the inward oriented protomers, suggesting that membrane deformations occur during transport. | |||
Structural ensemble of a glutamate transporter homologue in lipid nanodisc environment.,Arkhipova V, Guskov A, Slotboom DJ Nat Commun. 2020 Feb 21;11(1):998. doi: 10.1038/s41467-020-14834-8. PMID:32081874<ref>PMID:32081874</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6xwp" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Arkhipova, V]] | |||
[[Category: Guskov, A]] | |||
[[Category: Slotboom, D J]] | |||
[[Category: Amino acid transporter]] | |||
[[Category: Aspartate transport]] | |||
[[Category: Glutamate transporter homologue]] | |||
[[Category: Membrane protein]] | |||
[[Category: Transport protein]] | |||
Revision as of 06:59, 4 March 2020
Structure of glutamate transporter homologue GltTk in unsaturated conditions - outward-outward-inward configuration
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