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1K4C

Potassium Channel KcsA-Fab complex in high concentration of K+

1K4C の概要
エントリーDOI10.2210/pdb1k4c/pdb
分子名称antibody Fab fragment heavy chain, antibody Fab fragment light chain, potassium channel KcsA, ... (7 entities in total)
機能のキーワードk channel, protein-antibody fab complex, membrane protein
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61101.52
構造登録者
Zhou, Y.,Morais-Cabral, J.H.,Kaufman, A.,MacKinnon, R. (登録日: 2001-10-07, 公開日: 2001-11-14, 最終更新日: 2024-10-30)
主引用文献Zhou, Y.,Morais-Cabral, J.H.,Kaufman, A.,MacKinnon, R.
Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution.
Nature, 414:43-48, 2001
Cited by
PubMed Abstract: Ion transport proteins must remove an ion's hydration shell to coordinate the ion selectively on the basis of its size and charge. To discover how the K+ channel solves this fundamental aspect of ion conduction, we solved the structure of the KcsA K+ channel in complex with a monoclonal Fab antibody fragment at 2.0 A resolution. Here we show how the K+ channel displaces water molecules around an ion at its extracellular entryway, and how it holds a K+ ion in a square antiprism of water molecules in a cavity near its intracellular entryway. Carbonyl oxygen atoms within the selectivity filter form a very similar square antiprism around each K+ binding site, as if to mimic the waters of hydration. The selectivity filter changes its ion coordination structure in low K+ solutions. This structural change is crucial to the operation of the selectivity filter in the cellular context, where the K+ ion concentration near the selectivity filter varies in response to channel gating.
PubMed: 11689936
DOI: 10.1038/35102009
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2 Å)
構造検証レポート
Validation report summary of 1k4c
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2025-06-18に公開中

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