5NKQ の概要
| エントリーDOI | 10.2210/pdb5nkq/pdb |
| 分子名称 | Putative fluoride ion transporter CrcB, Monobody, SODIUM ION, ... (5 entities in total) |
| 機能のキーワード | dual topology channel, fluoride channel, monobody, transport protein |
| 由来する生物種 | Bordetella pertussis 詳細 |
| 細胞内の位置 | Cell inner membrane ; Multi-pass membrane protein : Q7VYU0 |
| タンパク質・核酸の鎖数 | 8 |
| 化学式量合計 | 93816.90 |
| 構造登録者 | |
| 主引用文献 | Stockbridge, R.B.,Kolmakova-Partensky, L.,Shane, T.,Koide, A.,Koide, S.,Miller, C.,Newstead, S. Crystal structures of a double-barrelled fluoride ion channel. Nature, 525:548-551, 2015 Cited by PubMed Abstract: To contend with hazards posed by environmental fluoride, microorganisms export this anion through F(-)-specific ion channels of the Fluc family. Since the recent discovery of Fluc channels, numerous idiosyncratic features of these proteins have been unearthed, including strong selectivity for F(-) over Cl(-) and dual-topology dimeric assembly. To understand the chemical basis for F(-) permeation and how the antiparallel subunits convene to form a F(-)-selective pore, here we solve the crystal structures of two bacterial Fluc homologues in complex with three different monobody inhibitors, with and without F(-) present, to a maximum resolution of 2.1 Å. The structures reveal a surprising 'double-barrelled' channel architecture in which two F(-) ion pathways span the membrane, and the dual-topology arrangement includes a centrally coordinated cation, most likely Na(+). F(-) selectivity is proposed to arise from the very narrow pores and an unusual anion coordination that exploits the quadrupolar edges of conserved phenylalanine rings. PubMed: 26344196DOI: 10.1038/nature14981 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.17 Å) |
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