6CTF

Crystal structure of GltPh fast mutant - R276S/M395R

6CTF の概要

• エントリーDOI: 10.2210/pdb6ctf/pdb
• 分子名称: Glutamate transporter homolog, ASPARTIC ACID, SODIUM ION (3 entities in total)
• 機能のキーワード: transporter, ligand-bound, membrane protein
• 由来する生物種: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 130513.06

構造登録者

Boudker, O.,Oh, S. (登録日: 2018-03-23, 公開日: 2018-10-10, 最終更新日: 2024-10-23)

主引用文献

Oh, S.,Boudker, O.
Kinetic mechanism of coupled binding in sodium-aspartate symporter GltPh.
Elife, 7:-, 2018

PubMed Abstract: Many secondary active membrane transporters pump substrates against concentration gradients by coupling their uptake to symport of sodium ions. Symport requires the substrate and ions to be always transported together. Cooperative binding of the solutes is a key mechanism contributing to coupled transport in the sodium and aspartate symporter from Glt. Here, we describe the kinetic mechanism of coupled binding for Glt in the inward facing state. The first of the three coupled sodium ions, binds weakly and slowly, enabling the protein to accept the rest of the ions and the substrate. The last ion binds tightly, but is in rapid equilibrium with solution. Its release is required for the complex disassembly. Thus, the first ion serves to 'open the door' for the substrate, the last ion 'locks the door' once the substrate is in, and one ion contributes to both events.

PubMed: 30255846
DOI: 10.7554/eLife.37291

実験手法

X-RAY DIFFRACTION (4.05 Å)