8HTI

Human Consensus Olfactory Receptor OR52c in Complex with Octanoic Acid (OCA) and G Protein

Summary for 8HTI

• Entry DOI: 10.2210/pdb8hti/pdb
• EMDB information: 35010
• Descriptor: Guanine nucleotide-binding protein G(s) subunit alpha isoforms short, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2, ... (6 entities in total)
• Functional Keywords: olfactory receptor, g protein, membrane protein, gpcr, olfactory gpcr
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 5
• Total formula weight: 144822.55

Authors

Choi, C.W.,Bae, J.,Choi, H.-J.,Kim, J. (deposition date: 2022-12-21, release date: 2023-12-20)

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

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

Experimental method

ELECTRON MICROSCOPY (2.97 Å)