1K4C
Potassium Channel KcsA-Fab complex in high concentration of K+
1K4C の概要
エントリーDOI | 10.2210/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: 11689936DOI: 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) |
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