6xwo

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'''Unreleased structure'''
 
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The entry 6xwo is ON HOLD until Paper Publication
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==Structure of glutamate transporter homologue GltTk in the unsaturated conditions - inward-inward-outward configuration==
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<StructureSection load='6xwo' size='340' side='right'caption='[[6xwo]], [[Resolution|resolution]] 3.39&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6xwo]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XWO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6XWO FirstGlance]. <br>
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</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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6xwq|6xwq]], [[6xwp|6xwp]], [[6xwn|6xwn]], [[6xwr|6xwr]]</td></tr>
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<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=6xwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xwo OCA], [http://pdbe.org/6xwo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6xwo RCSB], [http://www.ebi.ac.uk/pdbsum/6xwo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6xwo ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6xwo" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Arkhipova, V]]
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[[Category: Guskov, A]]
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[[Category: Slotboom, D J]]
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[[Category: Amino acid transporter]]
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[[Category: Aspartate transport]]
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[[Category: Glutamate transporter homologue]]
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[[Category: Membrane protein]]
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[[Category: Transport protein]]

Revision as of 06:59, 4 March 2020

Structure of glutamate transporter homologue GltTk in the unsaturated conditions - inward-inward-outward configuration

PDB ID 6xwo

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