View source for 6hjy


==X-ray structure of a pentameric ligand gated ion channel from Erwinia chrysanthemi (ELIC) Delta8 truncation mutant in complex with nanobody 72==
<StructureSection load='6hjy' size='340' side='right'caption='[[6hjy]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6hjy]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Dickeya_chrysanthemi Dickeya chrysanthemi] and [https://en.wikipedia.org/wiki/Lama_glama Lama glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HJY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HJY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.78&#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=6hjy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hjy OCA], [https://pdbe.org/6hjy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hjy RCSB], [https://www.ebi.ac.uk/pdbsum/6hjy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hjy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ELIC_DICCH ELIC_DICCH] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Phospholipids are key components of cellular membranes and are emerging as important functional regulators of different membrane proteins, including pentameric ligand-gated ion channels (pLGICs). Here, we take advantage of the prokaryote channel ELIC (Erwinia ligand-gated ion channel) as a model to understand the determinants of phospholipid interactions in this family of receptors. A high-resolution structure of ELIC in a lipid-bound state reveals a phospholipid site at the lower half of pore-forming transmembrane helices M1 and M4 and at a nearby site for neurosteroids, cholesterol or general anesthetics. This site is shaped by an M4-helix kink and a Trp-Arg-Pro triad that is highly conserved in eukaryote GABAA/C and glycine receptors. A combined approach reveals that M4 is intrinsically flexible and that M4 deletions or disruptions of the lipid-binding site accelerate desensitization in ELIC, suggesting that lipid interactions shape the agonist response. Our data offer a structural context for understanding lipid modulation in pLGICs.

A lipid site shapes the agonist response of a pentameric ligand-gated ion channel.,Henault CM, Govaerts C, Spurny R, Brams M, Estrada-Mondragon A, Lynch J, Bertrand D, Pardon E, Evans GL, Woods K, Elberson BW, Cuello LG, Brannigan G, Nury H, Steyaert J, Baenziger JE, Ulens C Nat Chem Biol. 2019 Oct 7. pii: 10.1038/s41589-019-0369-4. doi:, 10.1038/s41589-019-0369-4. PMID:31591563<ref>PMID:31591563</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6hjy" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ion channels 3D structures|Ion channels 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Dickeya chrysanthemi]]
[[Category: Lama glama]]
[[Category: Large Structures]]
[[Category: Evans GL]]
[[Category: Govaerts C]]
[[Category: Pardon E]]
[[Category: Spurny R]]
[[Category: Steyaert J]]
[[Category: Ulens C]]