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-Structure paper
タイトル | Structure of the mechanosensitive OSCA channels. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 25, Issue 9, Page 850-858, Year 2018 |
掲載日 | 2018年9月6日 |
著者 | Mingfeng Zhang / Dali Wang / Yunlu Kang / Jing-Xiang Wu / Fuqiang Yao / Chengfang Pan / Zhiqiang Yan / Chen Song / Lei Chen / |
PubMed 要旨 | Mechanosensitive ion channels convert mechanical stimuli into a flow of ions. These channels are widely distributed from bacteria to higher plants and humans, and are involved in many crucial ...Mechanosensitive ion channels convert mechanical stimuli into a flow of ions. These channels are widely distributed from bacteria to higher plants and humans, and are involved in many crucial physiological processes. Here we show that two members of the OSCA protein family in Arabidopsis thaliana, namely AtOSCA1.1 and AtOSCA3.1, belong to a new class of mechanosensitive ion channels. We solve the structure of the AtOSCA1.1 channel at 3.5-Å resolution and AtOSCA3.1 at 4.8-Å resolution by cryo-electron microscopy. OSCA channels are symmetric dimers that are mediated by cytosolic inter-subunit interactions. Strikingly, they have structural similarity to the mammalian TMEM16 family proteins. Our structural analysis accompanied with electrophysiological studies identifies the ion permeation pathway within each subunit and suggests a conformational change model for activation. |
リンク | Nat Struct Mol Biol / PubMed:30190597 |
手法 | EM (単粒子) |
解像度 | 3.52 - 4.8 Å |
構造データ | |
由来 |
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キーワード | METAL TRANSPORT / osca / TMEM63 / ion channel / mechanosensitive / membrane protein / osmosensing |