8EOW

Eag Kv channel with voltage sensor in the up conformation

8EOW の概要

• エントリーDOI: 10.2210/pdb8eow/pdb
• 関連するPDBエントリー: 8EP0 8EP1
• EMDBエントリー: 28487 28494 28498
• 分子名称: Potassium voltage-gated channel subfamily H member 1, Calmodulin-1 (2 entities in total)
• 機能のキーワード: voltage-gated potassium channel, membrane protein
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 390910.81

構造登録者

Mandala, V.S.,MacKinnon, R. (登録日: 2022-10-04, 公開日: 2022-11-16, 最終更新日: 2025-06-04)

主引用文献

Mandala, V.S.,MacKinnon, R.
Voltage-sensor movements in the Eag Kv channel under an applied electric field.
Proc.Natl.Acad.Sci.USA, 119:e2214151119-e2214151119, 2022

PubMed Abstract: Voltage-dependent ion channels regulate the opening of their pores by sensing the membrane voltage. This process underlies the propagation of action potentials and other forms of electrical activity in cells. The voltage dependence of these channels is governed by the transmembrane displacement of the positive charged S4 helix within their voltage-sensor domains. We use cryo-electron microscopy to visualize this movement in the mammalian Eag voltage-dependent potassium channel in lipid membrane vesicles with a voltage difference across the membrane. Multiple structural configurations show that the applied electric field displaces S4 toward the cytoplasm by two helical turns, resulting in an extended interfacial helix near the inner membrane leaflet. The position of S4 in this down conformation is sterically incompatible with an open pore, thus explaining how movement of the voltage sensor at hyperpolarizing membrane voltages locks the pore shut in this kind of voltage-dependent K (K) channel. The structures solved in lipid bilayer vesicles detail the intricate interplay between K channels and membranes, from showing how arginines are stabilized deep within the membrane and near phospholipid headgroups, to demonstrating how the channel reshapes the inner leaflet of the membrane itself.

PubMed: 36331999
DOI: 10.1073/pnas.2214151119

実験手法

ELECTRON MICROSCOPY (3.9 Å)