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3IFX

Crystal structure of the Spin-labeled KcsA mutant V48R1

3IFX の概要
エントリーDOI10.2210/pdb3ifx/pdb
分子名称Voltage-gated potassium channel, POTASSIUM ION, S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate, ... (5 entities in total)
機能のキーワードpotassium channel, spin-labeled protein, membrane protein, cell membrane, ion transport, ionic channel, membrane, transmembrane, transport, voltage-gated channel
由来する生物種Streptomyces lividans
細胞内の位置Cell membrane; Multi-pass membrane protein: P0A334
タンパク質・核酸の鎖数4
化学式量合計57147.72
構造登録者
Cieslak, J.A.,Focia, P.J.,Gross, A. (登録日: 2009-07-26, 公開日: 2010-02-09, 最終更新日: 2024-11-20)
主引用文献Cieslak, J.A.,Focia, P.J.,Gross, A.
Electron Spin-Echo Envelope Modulation (ESEEM) Reveals Water and Phosphate Interactions with the KcsA Potassium Channel
Biochemistry, 49:1486-1494, 2010
Cited by
PubMed Abstract: Electron spin-echo envelope modulation (ESEEM) spectroscopy is a well-established technique for the study of naturally occurring paramagnetic metal centers. The technique has been used to study copper complexes, hemes, enzyme mechanisms, micellar water content, and water permeation profiles in membranes, among other applications. In the present study, we combine ESEEM spectroscopy with site-directed spin labeling (SDSL) and X-ray crystallography in order to evaluate the technique's potential as a structural tool to describe the native environment of membrane proteins. Using the KcsA potassium channel as a model system, we demonstrate that deuterium ESEEM can detect water permeation along the lipid-exposed surface of the KcsA outer helix. We further demonstrate that (31)P ESEEM is able to identify channel residues that interact with the phosphate headgroup of the lipid bilayer. In combination with X-ray crystallography, the (31)P data may be used to define the phosphate interaction surface of the protein. The results presented here establish ESEEM as a highly informative technique for SDSL studies of membrane proteins.
PubMed: 20092291
DOI: 10.1021/bi9016523
主引用文献が同じPDBエントリー
実験手法
EPR
X-RAY DIFFRACTION (3.56 Å)
構造検証レポート
Validation report summary of 3ifx
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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