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-Structure paper
Title | Structure of the hyperosmolality-gated calcium-permeable channel OSCA1.2. |
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Journal, issue, pages | Nat Commun, Vol. 9, Issue 1, Page 5060, Year 2018 |
Publish date | Nov 29, 2018 |
![]() | Xin Liu / Jiawei Wang / Linfeng Sun / ![]() |
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 ...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. |
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Methods | EM (single particle) |
Resolution | 3.68 - 5.4 Å |
Structure data | ![]() EMDB-9677: |
Source |
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![]() | MEMBRANE PROTEIN / Channel |