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TitleStructure of the mechanosensitive OSCA channels.
Journal, issue, pagesNat Struct Mol Biol, Vol. 25, Issue 9, Page 850-858, Year 2018
Publish dateSep 6, 2018
AuthorsMingfeng Zhang / Dali Wang / Yunlu Kang / Jing-Xiang Wu / Fuqiang Yao / Chengfang Pan / Zhiqiang Yan / Chen Song / Lei Chen /
PubMed AbstractMechanosensitive 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.
External linksNat Struct Mol Biol / PubMed:30190597
MethodsEM (single particle)
Resolution3.52 - 4.8 Å
Structure data

6822

6jpf

EMDB-6822: Structure of atOSCA1.1 channel
PDB-6jpf: Structure of atOSCA1.1 channel at 3.52A
Method: EM (single particle) / Resolution: 3.52 Å

6875

5z1f

EMDB-6875, PDB-5z1f:
Structure of atOSCA3.1 channel
Method: EM (single particle) / Resolution: 4.8 Å

Source
  • arabidopsis thaliana (thale cress)
KeywordsMETAL TRANSPORT / osca / TMEM63 / ion channel / mechanosensitive / membrane protein / osmosensing

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