View source for 9h95


==YnaI in closed conformation purified in DDM with additional lipids showing ligand-filled pockets==
<StructureSection load='9h95' size='340' side='right'caption='[[9h95]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9h95]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9H95 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9H95 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D12:DODECANE'>D12</scene></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=9h95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9h95 OCA], [https://pdbe.org/9h95 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9h95 RCSB], [https://www.ebi.ac.uk/pdbsum/9h95 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9h95 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/YNAI_ECO57 YNAI_ECO57] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Osmotically varying environments are challenging for bacterial cells. Sudden drops in osmolytes cause an increased membrane tension and rupture the cells in the absence of protective mechanisms. One family of protective proteins are mechanosensitive channels of small conductance that open in response to membrane tension. Although these channels have a common architecture, they vary widely in the number of transmembrane helices, conductivity, and gating characteristics. Although there are various structures of channels in the open and closed state, the underlying common principles of the gating mechanism remain poorly understood. Here we show that YnaI opens by radial relocation of the transmembrane sensor paddles together with a shortening of the pore, which contrasts the prototypic smaller MscS. A chimera of both channels with the YnaI sensor paddles and the pore containing C-terminal part of MscS is functional and has the tension response of the paddle donor. Our research shows that elements with different structural opening mechanisms can be mixed and matched within one channel as long as they support the common area expansion on the periplasmic side.

Mechanosensitive channel engineering: A study on the mixing and matching of YnaI and MscS sensor paddles and pores.,Flegler VJ, Rasmussen A, Hedrich R, Rasmussen T, Bottcher B Nat Commun. 2025 Aug 23;16(1):7881. doi: 10.1038/s41467-025-63253-0. PMID:40849500<ref>PMID:40849500</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9h95" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Bottcher B]]
[[Category: Flegler VJ]]
[[Category: Hedrich R]]
[[Category: Rasmussen A]]
[[Category: Rasmussen T]]