View source for 8j46


==Human Consensus Olfactory Receptor OR52c in apo state, OR52c-bRIL==
<StructureSection load='8j46' size='340' side='right'caption='[[8j46]], [[Resolution|resolution]] 3.66&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8j46]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8J46 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8J46 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]] 3.66&#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=8j46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8j46 OCA], [https://pdbe.org/8j46 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8j46 RCSB], [https://www.ebi.ac.uk/pdbsum/8j46 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8j46 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX] Electron-transport protein of unknown function.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Structural and mechanistic studies on human odorant receptors (ORs), key in olfactory signaling, are challenging because of their low surface expression in heterologous cells. The recent structure of OR51E2 bound to propionate provided molecular insight into odorant recognition, but the lack of an inactive OR structure limited understanding of the activation mechanism of ORs upon odorant binding. Here, we determined the cryo-electron microscopy structures of consensus OR52 (OR52(cs)), a representative of the OR52 family, in the ligand-free (apo) and octanoate-bound states. The apo structure of OR52(cs) reveals a large opening between transmembrane helices (TMs) 5 and 6. A comparison between the apo and active structures of OR52(cs) demonstrates the inward and outward movements of the extracellular and intracellular segments of TM6, respectively. These results, combined with molecular dynamics simulations and signaling assays, shed light on the molecular mechanisms of odorant binding and activation of the OR52 family.

Understanding the molecular mechanisms of odorant binding and activation of the human OR52 family.,Choi C, Bae J, Kim S, Lee S, Kang H, Kim J, Bang I, Kim K, Huh WK, Seok C, Park H, Im W, Choi HJ Nat Commun. 2023 Dec 7;14(1):8105. doi: 10.1038/s41467-023-43983-9. PMID:38062020<ref>PMID:38062020</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8j46" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bae J]]
[[Category: Choi CW]]
[[Category: Choi H-J]]
[[Category: Kim J]]