6UFE

The structure of a potassium selective ion channel at atomic resolution

6UFE の概要

• エントリーDOI: 10.2210/pdb6ufe/pdb
• 分子名称: Transporter, (4S)-2-METHYL-2,4-PENTANEDIOL, POTASSIUM ION, ... (4 entities in total)
• 機能のキーワード: ion channel, potassium ion channel, membrane protein
• 由来する生物種: Bacillus cereus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21886.43

構造登録者

Langan, P.S.,Vandavasi, V.G.,Sullivan, B.,Afonine, P.V.,Weiss, K.L. (登録日: 2019-09-24, 公開日: 2020-08-05, 最終更新日: 2023-10-11)

主引用文献

Langan, P.S.,Vandavasi, V.G.,Kopec, W.,Sullivan, B.,Afonne, P.V.,Weiss, K.L.,de Groot, B.L.,Coates, L.
The structure of a potassium-selective ion channel reveals a hydrophobic gate regulating ion permeation.
Iucrj, 7:835-843, 2020

PubMed Abstract: Protein dynamics are essential to function. One example of this is the various gating mechanisms within ion channels, which are transmembrane proteins that act as gateways into the cell. Typical ion channels switch between an open and closed state via a conformational transition which is often triggered by an external stimulus, such as ligand binding or pH and voltage differences. The atomic resolution structure of a potassium-selective ion channel named NaK2K has allowed us to observe that a hydro-phobic residue at the bottom of the selectivity filter, Phe92, appears in dual conformations. One of the two conformations of Phe92 restricts the diameter of the exit pore around the selectivity filter, limiting ion flow through the channel, while the other conformation of Phe92 provides a larger-diameter exit pore from the selectivity filter. Thus, it can be concluded that Phe92 acts as a hydro-phobic gate, regulating the flow of ions through the selectivity filter.

PubMed: 32939275
DOI: 10.1107/S2052252520008271

実験手法

X-RAY DIFFRACTION (1.2 Å)