6MGV
Structure of mechanically activated ion channel OSCA1.2 in nanodisc
6MGV の概要
エントリーDOI | 10.2210/pdb6mgv/pdb |
関連するPDBエントリー | 6MGW |
EMDBエントリー | 9112 9113 |
分子名称 | Calcium permeable stress-gated cation channel 1 (1 entity in total) |
機能のキーワード | mechanically activated ion channel, membrane protein |
由来する生物種 | Arabidopsis thaliana (Mouse-ear cress) |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 178063.44 |
構造登録者 | Jojoa-Cruz, S.,Saotome, K.,Patapoutian, A.,Ward, A.B. (登録日: 2018-09-15, 公開日: 2018-11-14, 最終更新日: 2024-03-13) |
主引用文献 | Jojoa Cruz, S.,Saotome, K.,Murthy, S.E.,Tsui, C.C.A.,Sansom, M.S.,Patapoutian, A.,Ward, A.B. Cryo-EM structure of the mechanically activated ion channel OSCA1.2. Elife, 7:-, 2018 Cited by PubMed Abstract: Mechanically activated ion channels underlie touch, hearing, shear-stress sensing, and response to turgor pressure. OSCA/TMEM63s are a newly-identified family of eukaryotic mechanically activated ion channels opened by membrane tension. The structural underpinnings of OSCA/TMEM63 function are not explored. Here, we elucidate high resolution cryo-electron microscopy structures of OSCA1.2, revealing a dimeric architecture containing eleven transmembrane helices per subunit and surprising topological similarities to TMEM16 proteins. We locate the ion permeation pathway within each subunit by demonstrating that a conserved acidic residue is a determinant of channel conductance. Molecular dynamics simulations reveal membrane interactions, suggesting the role of lipids in OSCA1.2 gating. These results lay a foundation to decipher how the structural organization of OSCA/TMEM63 is suited for their roles as MA ion channels. PubMed: 30382939DOI: 10.7554/eLife.41845 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.1 Å) |
構造検証レポート
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