4X8A

NavMS pore and C-terminal domain grown from protein purified in LiCl

4X8A の概要

• エントリーDOI: 10.2210/pdb4x8a/pdb
• 関連するPDBエントリー: 3ZJZ 4CBC 4X87 4X88 4X89
• 分子名称: Ion transport protein, HEGA-10, NONAETHYLENE GLYCOL, ... (5 entities in total)
• 機能のキーワード: transport protein, selectivity filter, membrane protein
• 由来する生物種: Magnetococcus sp. (strain MC-1)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 70601.87

構造登録者

Naylor, C.E.,Bagneris, C.,Wallace, B.A. (登録日: 2014-12-10, 公開日: 2016-03-09, 最終更新日: 2024-05-08)

主引用文献

Naylor, C.E.,Bagneris, C.,DeCaen, P.G.,Sula, A.,Scaglione, A.,Clapham, D.E.,Wallace, B.A.
Molecular basis of ion permeability in a voltage-gated sodium channel.
Embo J., 35:820-830, 2016

PubMed Abstract: Voltage-gated sodium channels are essential for electrical signalling across cell membranes. They exhibit strong selectivities for sodium ions over other cations, enabling the finely tuned cascade of events associated with action potentials. This paper describes the ion permeability characteristics and the crystal structure of a prokaryotic sodium channel, showing for the first time the detailed locations of sodium ions in the selectivity filter of a sodium channel. Electrostatic calculations based on the structure are consistent with the relative cation permeability ratios (Na(+) ≈ Li(+) ≫ K(+), Ca(2+), Mg(2+)) measured for these channels. In an E178D selectivity filter mutant constructed to have altered ion selectivities, the sodium ion binding site nearest the extracellular side is missing. Unlike potassium ions in potassium channels, the sodium ions in these channels appear to be hydrated and are associated with side chains of the selectivity filter residues, rather than polypeptide backbones.

PubMed: 26873592
DOI: 10.15252/embj.201593285

実験手法

X-RAY DIFFRACTION (3.02 Å)