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5yd1

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Current revision (06:59, 10 April 2019) (edit) (undo)
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#REDIRECT [[6jpf]] This PDB entry is obsolete and replaced by 6jpf
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==Structure of atOSCA1.1 channel==
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<StructureSection load='5yd1' size='340' side='right' caption='[[5yd1]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5yd1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YD1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YD1 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OSCA1, At4g04340, T19B17.6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
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<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=5yd1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yd1 OCA], [http://pdbe.org/5yd1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yd1 RCSB], [http://www.ebi.ac.uk/pdbsum/5yd1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yd1 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/CSCL5_ARATH 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(+).<ref>PMID:25162526</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:30190597</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5yd1" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Arath]]
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[[Category: Chen, L]]
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[[Category: Kang, Y]]
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[[Category: Wu, J X]]
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[[Category: Zhang, M]]
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[[Category: Ion channel]]
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[[Category: Mechanosensitive]]
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[[Category: Membrane protein]]
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[[Category: Metal transport]]
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[[Category: Osca]]
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[[Category: Osmosensing]]
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[[Category: Tmem63]]
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Current revision

  1. REDIRECT 6jpf This PDB entry is obsolete and replaced by 6jpf

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