6x3f
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==hEAAT3-IFS-Apo== | |
| + | <StructureSection load='6x3f' size='340' side='right'caption='[[6x3f]], [[Resolution|resolution]] 3.03Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6X3F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6X3F 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]] 3.03Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CHT:CHOLINE+ION'>CHT</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=6x3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x3f OCA], [https://pdbe.org/6x3f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6x3f RCSB], [https://www.ebi.ac.uk/pdbsum/6x3f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6x3f ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Human excitatory amino acid transporter 3 (hEAAT3) mediates glutamate uptake in neurons, intestine, and kidney. Here, we report cryo-EM structures of hEAAT3 in several functional states where the transporter is empty, bound to coupled sodium ions only, or fully loaded with three sodium ions, a proton, and the substrate aspartate. The structures suggest that hEAAT3 operates by an elevator mechanism involving three functionally independent subunits. When the substrate-binding site is near the cytoplasm, it has a remarkably low affinity for the substrate, perhaps facilitating its release and allowing the rapid transport turnover. The mechanism of the coupled uptake of the sodium ions and the substrate is conserved across evolutionarily distant families and is augmented by coupling to protons in EAATs. The structures further suggest a mechanism by which a conserved glutamate residue mediates proton symport. | ||
| - | + | Cryo-EM structures of excitatory amino acid transporter 3 visualize coupled substrate, sodium, and proton binding and transport.,Qiu B, Matthies D, Fortea E, Yu Z, Boudker O Sci Adv. 2021 Mar 3;7(10). pii: 7/10/eabf5814. doi: 10.1126/sciadv.abf5814. Print, 2021 Mar. PMID:33658209<ref>PMID:33658209</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6x3f" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Boudker O]] | ||
| + | [[Category: Matthies D]] | ||
| + | [[Category: Qiu B]] | ||
Current revision
hEAAT3-IFS-Apo
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