2X6B

Potassium Channel from Magnetospirillum Magnetotacticum

2X6B の概要

• エントリーDOI: 10.2210/pdb2x6b/pdb
• 関連するPDBエントリー: 1XL4 1XL6 2WLH 2WLI 2WLJ 2WLK 2WLL 2WLM 2WLN 2WLO 2X6A 2X6C
• 分子名称: ATP-SENSITIVE INWARD RECTIFIER POTASSIUM CHANNEL 10, BARIUM ION, POTASSIUM ION, ... (5 entities in total)
• 機能のキーワード: ion channel, metal transport, integral membrane protein
• 由来する生物種: MAGNETOSPIRILLUM MAGNETOTACTICUM
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34164.49

構造登録者

Clarke, O.B.,Caputo, A.T.,Hill, A.P.,Vandenberg, J.I.,Smith, B.J.,Gulbis, J.M. (登録日: 2010-02-15, 公開日: 2010-06-23, 最終更新日: 2023-12-20)

主引用文献

Clarke, O.B.,Caputo, A.T.,Hill, A.P.,Vandenberg, J.I.,Smith, B.J.,Gulbis, J.M.
Domain Reorientation and Rotation of an Intracellular Assembly Regulate Conduction in Kir Potassium Channels.
Cell(Cambridge,Mass.), 141:1018-, 2010

PubMed Abstract: Potassium channels embedded in cell membranes employ gates to regulate K+ current. While a specific constriction in the permeation pathway has historically been implicated in gating, recent reports suggest that the signature ion selectivity filter located in the outer membrane leaflet may be equally important. Inwardly rectifying K+ channels also control the directionality of flow, using intracellular polyamines to stem ion efflux by a valve-like action. This study presents crystallographic evidence of interdependent gates in the conduction pathway and reveals the mechanism of polyamine block. Reorientation of the intracellular domains, concomitant with activation, instigates polyamine release from intracellular binding sites to block the permeation pathway. Conformational adjustments of the slide helices, achieved by rotation of the cytoplasmic assembly relative to the pore, are directly correlated to the ion configuration in the selectivity filter. Ion redistribution occurs irrespective of the constriction, suggesting a more expansive role of the selectivity filter in gating than previously appreciated.

PubMed: 20564790
DOI: 10.1016/J.CELL.2010.05.003

実験手法

X-RAY DIFFRACTION (3.3 Å)