9BH1
Apo GltPh, intermediate outward-facing state
Summary for 9BH1
| Entry DOI | 10.2210/pdb9bh1/pdb |
| EMDB information | 44529 |
| Descriptor | Glutamate transporter homolog (1 entity in total) |
| Functional Keywords | sodium-coupled aspartate transporter, transport protein |
| Biological source | Pyrococcus horikoshii |
| Total number of polymer chains | 1 |
| Total formula weight | 44641.94 |
| Authors | |
| Primary citation | Reddy, K.D.,Rasool, B.,Akher, F.B.,Kutlesic, N.,Pant, S.,Boudker, O. Evolutionary analysis reveals the origin of sodium coupling in glutamate transporters. Biorxiv, 2024 Cited by PubMed Abstract: 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. PubMed: 38106174DOI: 10.1101/2023.12.03.569786 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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