8W77
Human Consensus Olfactory Receptor OR52c in apo state, OR52c only
Summary for 8W77
Entry DOI | 10.2210/pdb8w77/pdb |
EMDB information | 35971 37336 |
Descriptor | Human Consensus Olfactory Receptor OR52c in apo state, receptor only,Soluble cytochrome b562 (1 entity in total) |
Functional Keywords | olfactory receptor, g protein, membrane protein, gpcr, olfactory gpcr |
Biological source | Homo sapiens More |
Total number of polymer chains | 1 |
Total formula weight | 49480.33 |
Authors | Choi, C.W.,Bae, J.,Choi, H.-J.,Kim, J. (deposition date: 2023-08-30, release date: 2023-12-20, Last modification date: 2024-10-23) |
Primary citation | Choi, C.,Bae, J.,Kim, S.,Lee, S.,Kang, H.,Kim, J.,Bang, I.,Kim, K.,Huh, W.K.,Seok, C.,Park, H.,Im, W.,Choi, H.J. Understanding the molecular mechanisms of odorant binding and activation of the human OR52 family. Nat Commun, 14:8105-8105, 2023 Cited by PubMed Abstract: 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), a representative of the OR52 family, in the ligand-free (apo) and octanoate-bound states. The apo structure of OR52 reveals a large opening between transmembrane helices (TMs) 5 and 6. A comparison between the apo and active structures of OR52 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. PubMed: 38062020DOI: 10.1038/s41467-023-43983-9 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.61 Å) |
Structure validation
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