View source for 6xwr


==Structure of glutamate transporter homologue GltTk in sodium only condition==
<SX load='6xwr' size='340' side='right' viewer='molstar' caption='[[6xwr]], [[Resolution|resolution]] 3.22&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6xwr]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_kodakarensis_KOD1 Thermococcus kodakarensis KOD1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XWR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XWR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.22&#8491;</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=6xwr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xwr OCA], [https://pdbe.org/6xwr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xwr RCSB], [https://www.ebi.ac.uk/pdbsum/6xwr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xwr ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/Q5JID0_THEKO Q5JID0_THEKO] 
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6xwr" style="background-color:#fffaf0;"></div>

==See Also==
*[[Symporter 3D structures|Symporter 3D structures]]
== References ==
<references/>
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[[Category: Large Structures]]
[[Category: Thermococcus kodakarensis KOD1]]
[[Category: Arkhipova V]]
[[Category: Guskov A]]
[[Category: Slotboom DJ]]