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4QE7

Open MthK pore structure soaked in 10 mM Ba2+/100 mM Na+

4QE7 の概要
エントリーDOI10.2210/pdb4qe7/pdb
関連するPDBエントリー3LDC 3LDD 3LDE 4QE9
分子名称Calcium-gated potassium channel MthK, BARIUM ION (3 entities in total)
機能のキーワードtransmembrane, ion channel, open conformation, transport protein
由来する生物種Methanothermobacter thermautotrophicus
細胞内の位置Cell membrane; Multi-pass membrane protein: O27564
タンパク質・核酸の鎖数1
化学式量合計9347.43
構造登録者
Guo, R.,Zeng, W.,Cui, H.,Chen, L.,Ye, S. (登録日: 2014-05-15, 公開日: 2014-07-09, 最終更新日: 2023-11-08)
主引用文献Guo, R.,Zeng, W.,Cui, H.,Chen, L.,Ye, S.
Ionic interactions of Ba2+ blockades in the MthK K+ channel
J.Gen.Physiol., 144:193-200, 2014
Cited by
PubMed Abstract: The movement and interaction of multiple ions passing through in single file underlie various fundamental K(+) channel properties, from the effective conduction of K(+) ions to channel blockade by Ba(2+) ions. In this study, we used single-channel electrophysiology and x-ray crystallography to probe the interactions of Ba(2+) with permeant ions within the ion conduction pathway of the MthK K(+) channel. We found that, as typical of K(+) channels, the MthK channel was blocked by Ba(2+) at the internal side, and the Ba(2+)-blocking effect was enhanced by external K(+). We also obtained crystal structures of the MthK K(+) channel pore in both Ba(2+)-Na(+) and Ba(2+)-K(+) environments. In the Ba(2+)-Na(+) environment, we found that a single Ba(2+) ion remained bound in the selectivity filter, preferably at site 2, whereas in the Ba(2+)-K(+) environment, Ba(2+) ions were predominantly distributed between sites 3 and 4. These ionic configurations are remarkably consistent with the functional studies and identify a molecular basis for Ba(2+) blockade of K(+) channels.
PubMed: 25024268
DOI: 10.1085/jgp.201411192
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.4 Å)
構造検証レポート
Validation report summary of 4qe7
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2026-04-15に公開中

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