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6IJZ

Structure of a plant cation channel

6IJZ の概要
エントリーDOI10.2210/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
Sun, L.,Wang, J.,Liu, X. (登録日: 2018-10-12, 公開日: 2018-12-12, 最終更新日: 2024-03-27)
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: 30498218
DOI: 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)
構造検証レポート
Validation report summary of 6ijz
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-13に公開中

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