| Literature DB >> 30190597 |
Mingfeng Zhang1,2,3, Dali Wang4, Yunlu Kang1, Jing-Xiang Wu1,2, Fuqiang Yao5, Chengfang Pan5, Zhiqiang Yan6, Chen Song7,8,9, Lei Chen10,11.
Abstract
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.Entities:
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Year: 2018 PMID: 30190597 DOI: 10.1038/s41594-018-0117-6
Source DB: PubMed Journal: Nat Struct Mol Biol ISSN: 1545-9985 Impact factor: 15.369