9bgz
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Ancestral uncoupled aspartate transporter, apo conditions, high-affinity state== | |
| + | <StructureSection load='9bgz' size='340' side='right'caption='[[9bgz]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9bgz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9BGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9BGZ 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]] 3Å</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=9bgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9bgz OCA], [https://pdbe.org/9bgz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9bgz RCSB], [https://www.ebi.ac.uk/pdbsum/9bgz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9bgz ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Secondary active membrane transporters harness the energy of ion gradients to concentrate their substrates. Homologous transporters evolved to couple transport to different ions in response to changing environments and needs. The bases of such diversification, and thus principles of ion coupling, are unexplored. Employing phylogenetics and ancestral protein reconstruction, we investigated sodium-coupled transport in prokaryotic glutamate transporters, a mechanism ubiquitous across life domains and critical to neurotransmitter recycling in humans. We found that the evolutionary transition from sodium-dependent to independent substrate binding to the transporter preceded changes in the coupling mechanism. Structural and functional experiments suggest that the transition entailed allosteric mutations, making sodium binding dispensable without affecting ion-binding sites. Allosteric tuning of transporters' energy landscapes might be a widespread route of their functional diversification. | ||
| - | + | Evolutionary analysis reveals the origin of sodium coupling in glutamate transporters.,Reddy KD, Rasool B, Akher FB, Kutlesic N, Pant S, Boudker O bioRxiv [Preprint]. 2024 Apr 25:2023.12.03.569786. doi: , 10.1101/2023.12.03.569786. PMID:38106174<ref>PMID:38106174</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Boudker | + | <div class="pdbe-citations 9bgz" style="background-color:#fffaf0;"></div> |
| - | [[Category: Reddy | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Boudker O]] | ||
| + | [[Category: Reddy KD]] | ||
Current revision
Ancestral uncoupled aspartate transporter, apo conditions, high-affinity state
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