View source for 8tdl


==Cryo-EM structure of the wild-type AtMSL10 in saposin==
<StructureSection load='8tdl' size='340' side='right'caption='[[8tdl]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8tdl]] is a 7 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=8TDL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8TDL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8tdl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8tdl OCA], [https://pdbe.org/8tdl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8tdl RCSB], [https://www.ebi.ac.uk/pdbsum/8tdl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8tdl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MSL10_ARATH MSL10_ARATH] Mechanosensitive channel that opens in response to stretch forces in the membrane lipid bilayer.<ref>PMID:18485707</ref> <ref>PMID:19704841</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Plants are challenged by drastically different osmotic environments during growth and development. Adaptation to these environments often involves mechanosensitive ion channels that can detect and respond to mechanical force. In the model plant Arabidopsis thaliana, the mechanosensitive channel MSL10 plays a crucial role in hypo-osmotic shock adaptation and programmed cell death induction, but the molecular basis of channel function remains poorly understood. Here, we report a structural and electrophysiological analysis of MSL10. The cryo-electron microscopy structures reveal a distinct heptameric channel assembly. Structures of the wild-type channel in detergent and lipid environments, and in the absence of membrane tension, capture an open conformation. Furthermore, structural analysis of a non-conductive mutant channel demonstrates that reorientation of phenylalanine side chains alone, without main chain rearrangements, may generate the hydrophobic gate. Together, these results reveal a distinct gating mechanism and advance our understanding of mechanotransduction.

Open structure and gating of the Arabidopsis mechanosensitive ion channel MSL10.,Zhang J, Maksaev G, Yuan P Nat Commun. 2023 Oct 7;14(1):6284. doi: 10.1038/s41467-023-42117-5. PMID:37805510<ref>PMID:37805510</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8tdl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Yuan P]]
[[Category: Zhang J]]