6jpf
From Proteopedia
Structure of atOSCA1.1 channel at 3.52A
Structural highlights
Function[CSCL5_ARATH] Acts as a hyperosmolarity-gated non-selective cation channel that permeates Ca(2+) ions. Shows the following permeability sequence: K(+) > Ba(2+) = Ca(2+) > Na(+) = Mg(2+) = Cs(+).[1] Publication Abstract from PubMedMechanosensitive 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-A resolution and AtOSCA3.1 at 4.8-A 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. Structure of the mechanosensitive OSCA channels.,Zhang M, Wang D, Kang Y, Wu JX, Yao F, Pan C, Yan Z, Song C, Chen L Nat Struct Mol Biol. 2018 Sep;25(9):850-858. doi: 10.1038/s41594-018-0117-6. Epub, 2018 Sep 6. PMID:30190597[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Arath | Large Structures | Chen, L | Kang, Y | Wu, J X | Zhang, M | Ion channel | Mechanosensitive | Membrane protein | Metal transport | Osca | Osmosensing | Tmem63
