6IJZ
Structure of a plant cation channel
6IJZ の概要
エントリーDOI | 10.2210/pdb6ijz/pdb |
EMDBエントリー | 9682 |
分子名称 | Calcium permeable stress-gated cation channel 1 (1 entity in total) |
機能のキーワード | 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 | 175971.09 |
構造登録者 | |
主引用文献 | Liu, X.,Wang, J.,Sun, L. Structure of the hyperosmolality-gated calcium-permeable channel OSCA1.2. Nat Commun, 9:5060-5060, 2018 Cited by PubMed Abstract: In plants, hyperosmolality stimuli triggers opening of the osmosensitive channels, leading to a rapid downstream signaling cascade initiated by cytosolic calcium concentration elevation. Members of the OSCA family in Arabidopsis thaliana, identified as the hyperosmolality-gated calcium-permeable channels, have been suggested to play a key role during the initial phase of hyperosmotic stress response. Here, we report the atomic structure of Arabidopsis OSCA1.2 determined by single-particle cryo-electron microscopy. It contains 11 transmembrane helices and forms a homodimer. It is in an inactivated state, and the pore-lining residues are clearly identified. Its cytosolic domain contains a RNA recognition motif and two unique long helices. The linker between these two helices forms an anchor in the lipid bilayer and may be essential to osmosensing. The structure of AtOSCA1.2 serves as a platform for the study of the mechanism underlying osmotic stress responses and mechanosensing. PubMed: 30498218DOI: 10.1038/s41467-018-07564-5 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.68 Å) |
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