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8W77

Human Consensus Olfactory Receptor OR52c in apo state, OR52c only

Summary for 8W77
Entry DOI10.2210/pdb8w77/pdb
EMDB information35971 37336
DescriptorHuman Consensus Olfactory Receptor OR52c in apo state, receptor only,Soluble cytochrome b562 (1 entity in total)
Functional Keywordsolfactory receptor, g protein, membrane protein, gpcr, olfactory gpcr
Biological sourceHomo sapiens
More
Total number of polymer chains1
Total formula weight49480.33
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 citationChoi, 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: 38062020
DOI: 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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