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TitleEvolutionary analysis reveals the origin of sodium coupling in glutamate transporters.
Journal, issue, pagesbioRxiv, Year 2024
Publish dateApr 25, 2024
AuthorsKrishna D Reddy / Burha Rasool / Farideh Badichi Akher / Nemanja Kutlešić / Swati Pant / Olga Boudker /
PubMed AbstractSecondary 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 ...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.
External linksbioRxiv / PubMed:38106174 / PubMed Central
MethodsEM (single particle)
Resolution2.7 - 3.4 Å
Structure data

44526

9bgy

EMDB-44526, PDB-9bgy:
Ancestral uncoupled aspartate transporter, apo conditions, low-affinity state
Method: EM (single particle) / Resolution: 3.0 Å

44527

9bgz

EMDB-44527, PDB-9bgz:
Ancestral uncoupled aspartate transporter, apo conditions, high-affinity state
Method: EM (single particle) / Resolution: 3.0 Å

44528

9bh0

EMDB-44528, PDB-9bh0:
Ancestral uncoupled aspartate transporter in complex with L-aspartate
Method: EM (single particle) / Resolution: 3.4 Å

44529

9bh1

EMDB-44529, PDB-9bh1:
Apo GltPh, intermediate outward-facing state
Method: EM (single particle) / Resolution: 3.1 Å

44530

9bh2

EMDB-44530, PDB-9bh2:
Apo GltPh, outward-facing state
Method: EM (single particle) / Resolution: 2.7 Å

Chemicals

ChemComp-ASP:
ASPARTIC ACID

Source
  • synthetic construct (others)
  • pyrococcus horikoshii (archaea)
KeywordsTRANSPORT PROTEIN / Transporter / ion-uncoupled / ancestral / Sodium-coupled aspartate transporter

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