1BL8
POTASSIUM CHANNEL (KCSA) FROM STREPTOMYCES LIVIDANS
1BL8 の概要
| エントリーDOI | 10.2210/pdb1bl8/pdb |
| 分子名称 | PROTEIN (POTASSIUM CHANNEL PROTEIN), POTASSIUM ION (3 entities in total) |
| 機能のキーワード | potassium channel, integral membrane protein, membrane protein |
| 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 | 41129.13 |
| 構造登録者 | Doyle, D.A.,Cabral, J.M.,Pfuetzner, R.A.,Kuo, A.,Gulbis, J.M.,Cohen, S.L.,Chait, B.T.,Mackinnon, R. (登録日: 1998-07-23, 公開日: 1998-07-29, 最終更新日: 2024-02-07) |
| 主引用文献 | Doyle, D.A.,Morais Cabral, J.,Pfuetzner, R.A.,Kuo, A.,Gulbis, J.M.,Cohen, S.L.,Chait, B.T.,MacKinnon, R. The structure of the potassium channel: molecular basis of K+ conduction and selectivity. Science, 280:69-77, 1998 Cited by PubMed Abstract: The potassium channel from Streptomyces lividans is an integral membrane protein with sequence similarity to all known K+ channels, particularly in the pore region. X-ray analysis with data to 3.2 angstroms reveals that four identical subunits create an inverted teepee, or cone, cradling the selectivity filter of the pore in its outer end. The narrow selectivity filter is only 12 angstroms long, whereas the remainder of the pore is wider and lined with hydrophobic amino acids. A large water-filled cavity and helix dipoles are positioned so as to overcome electrostatic destabilization of an ion in the pore at the center of the bilayer. Main chain carbonyl oxygen atoms from the K+ channel signature sequence line the selectivity filter, which is held open by structural constraints to coordinate K+ ions but not smaller Na+ ions. The selectivity filter contains two K+ ions about 7.5 angstroms apart. This configuration promotes ion conduction by exploiting electrostatic repulsive forces to overcome attractive forces between K+ ions and the selectivity filter. The architecture of the pore establishes the physical principles underlying selective K+ conduction. PubMed: 9525859DOI: 10.1126/science.280.5360.69 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.2 Å) |
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