6jpf | pdb_00006jpf

Structure of atOSCA1.1 channel at 3.52A

spinqualitylabelsall models 6jpf, resolution 3.52Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6jpf is a 2 chain structure. This structure supersedes the now removed PDB entry 5yd1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 5yd1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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(+). Publication Abstract from PubMed 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-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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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