9BH1

Apo GltPh, intermediate outward-facing state

9BH1 の概要

• エントリーDOI: 10.2210/pdb9bh1/pdb
• EMDBエントリー: 44529
• 分子名称: Glutamate transporter homolog (1 entity in total)
• 機能のキーワード: sodium-coupled aspartate transporter, transport protein
• 由来する生物種: Pyrococcus horikoshii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44641.94

構造登録者

Reddy, K.D.,Boudker, O. (登録日: 2024-04-19, 公開日: 2025-03-12)

主引用文献

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

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: 38106174
DOI: 10.1101/2023.12.03.569786

実験手法

ELECTRON MICROSCOPY (3.1 Å)