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8t57

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'''Unreleased structure'''
 
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The entry 8t57 is ON HOLD until Paper Publication
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==Structure of mechanically activated ion channel OSCA2.3 in peptidiscs==
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<StructureSection load='8t57' size='340' side='right'caption='[[8t57]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8t57]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8T57 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8T57 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8t57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8t57 OCA], [https://pdbe.org/8t57 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8t57 RCSB], [https://www.ebi.ac.uk/pdbsum/8t57 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8t57 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CSCLC_ARATH CSCLC_ARATH] Acts as an osmosensitive calcium-permeable cation channel.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Members of the OSCA/TMEM63 family are mechanically activated ion channels and structures of some OSCA members have revealed the architecture of these channels and structural features that are potentially involved in mechanosensation. However, these structures are all in a similar state and information about the motion of different elements of the structure is limited, preventing a deeper understanding of how these channels work. Here, we used cryoelectron microscopy to determine high-resolution structures of Arabidopsis thaliana OSCA1.2 and OSCA2.3 in peptidiscs. The structure of OSCA1.2 matches previous structures of the same protein in different environments. Yet, in OSCA2.3, the TM6a-TM7 linker adopts a different conformation that constricts the pore on its cytoplasmic side. Furthermore, coevolutionary sequence analysis uncovered a conserved interaction between the TM6a-TM7 linker and the beam-like domain (BLD). Our results reveal conformational heterogeneity and differences in conserved interactions between the TMD and BLD among members of the OSCA family.
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Authors:
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Structure of mechanically activated ion channel OSCA2.3 reveals mobile elements in the transmembrane domain.,Jojoa-Cruz S, Burendei B, Lee WH, Ward AB Structure. 2023 Dec 6:S0969-2126(23)00411-2. doi: 10.1016/j.str.2023.11.009. PMID:38103547<ref>PMID:38103547</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 8t57" 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: Arabidopsis thaliana]]
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[[Category: Large Structures]]
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[[Category: Burendei B]]
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[[Category: Jojoa-Cruz S]]
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[[Category: Lee WH]]
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[[Category: Ward AB]]

Revision as of 23:16, 27 December 2023

Structure of mechanically activated ion channel OSCA2.3 in peptidiscs

PDB ID 8t57

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