6IJZ

Structure of a plant cation channel

Summary for 6IJZ

• Entry DOI: 10.2210/pdb6ijz/pdb
• EMDB information: 9682
• Descriptor: Calcium permeable stress-gated cation channel 1 (1 entity in total)
• Functional Keywords: channel, membrane protein
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Total number of polymer chains: 2
• Total formula weight: 175971.09

Authors

Sun, L.,Wang, J.,Liu, X. (deposition date: 2018-10-12, release date: 2018-12-12, Last modification date: 2024-03-27)

Primary citation

Liu, X.,Wang, J.,Sun, L.
Structure of the hyperosmolality-gated calcium-permeable channel OSCA1.2.
Nat Commun, 9:5060-5060, 2018

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

Experimental method

ELECTRON MICROSCOPY (3.68 Å)