6ijz
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of a plant cation channel== | |
| + | <StructureSection load='6ijz' size='340' side='right' caption='[[6ijz]], [[Resolution|resolution]] 3.68Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6ijz]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IJZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IJZ FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ijz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ijz OCA], [http://pdbe.org/6ijz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ijz RCSB], [http://www.ebi.ac.uk/pdbsum/6ijz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ijz ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/CSC1_ARATH CSC1_ARATH]] Acts as an osmosensitive calcium-permeable cation channel. Specifically conducts cations including Ca(2+), K(+) and Na(+) in vitro. Inactivation or closure of the channel is calcium-dependent.<ref>PMID:24503647</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | Structure of the hyperosmolality-gated calcium-permeable channel OSCA1.2.,Liu X, Wang J, Sun L Nat Commun. 2018 Nov 29;9(1):5060. doi: 10.1038/s41467-018-07564-5. PMID:30498218<ref>PMID:30498218</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6ijz" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Liu, X]] | ||
| + | [[Category: Sun, L]] | ||
| + | [[Category: Wang, J]] | ||
| + | [[Category: Channel]] | ||
| + | [[Category: Membrane protein]] | ||
Revision as of 06:55, 12 December 2018
Structure of a plant cation channel
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Categories: Liu, X | Sun, L | Wang, J | Channel | Membrane protein
