2DWD

crystal structure of KcsA-FAB-TBA complex in Tl+

2DWD の概要

• エントリーDOI: 10.2210/pdb2dwd/pdb
• 関連するPDBエントリー: 1K4C 2DWE 2HVJ 2HVK
• 分子名称: ANTIBODY FAB HEAVY CHAIN, ANTIBODY FAB LIGHT CHAIN, Voltage-gated potassium channel, ... (8 entities in total)
• 機能のキーワード: potassium channel, membrane protein, tetrabutylammonium, k+, kcsa
• 由来する生物種: Streptomyces lividans; 詳細
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: P0A334
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 59444.58

構造登録者

Yohannan, S.,Zhou, Y. (登録日: 2006-08-10, 公開日: 2007-02-20, 最終更新日: 2024-11-20)

主引用文献

Yohannan, S.,Hu, Y.,Zhou, Y.
Crystallographic Study of the Tetrabutylammonium Block to the KcsA K(+) Channel
J.Mol.Biol., 366:806-814, 2007

PubMed Abstract: K(+) channels play essential roles in regulating membrane excitability of many diverse cell types by selectively conducting K(+) ions through their pores. Many diverse molecules can plug the pore and modulate the K(+) current. Quaternary ammonium (QA) ions are a class of pore blockers that have been used for decades by biophysicists to probe the pore, leading to important insights into the structure-function relation of K(+) channels. However, many key aspects of the QA-blocking mechanisms remain unclear to date, and understanding these questions requires high resolution structural information. Here, we address the question of whether intracellular QA blockade causes conformational changes of the K(+) channel selectivity filter. We have solved the structures of the KcsA K(+) channel in complex with tetrabutylammonium (TBA) and tetrabutylantimony (TBSb) under various ionic conditions. Our results demonstrate that binding of TBA or TBSb causes no significant change in the KcsA structure at high concentrations of permeant ions. We did observe the expected conformational change of the filter at low concentration of K(+), but this change appears to be independent of TBA or TBSb blockade.

PubMed: 17196615
DOI: 10.1016/j.jmb.2006.11.081

実験手法

X-RAY DIFFRACTION (2.6 Å)