9W45

The structure of odorant-bound mouse class II odorant receptor-miniGs complex

This is a non-PDB format compatible entry.

Summary for 9W45

• Entry DOI: 10.2210/pdb9w45/pdb
• EMDB information: 65621
• Descriptor: Guanine nucleotide-binding protein G(s) subunit alpha, 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: odorant receptor, membrane protein, membrane protein-immune system complex, membrane protein/immune system
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 5
• Total formula weight: 125968.33

Authors

Choi, C.W.,Gil, M.S.,Choi, H.-J. (deposition date: 2025-07-30, release date: 2026-03-04, Last modification date: 2026-05-06)

Primary citation

Gil, M.,Choi, C.,Kim, M.,Bae, M.,Lee, H.,Choi, I.,Im, W.,Choi, H.J.
Structural basis of odorant recognition by a mammalian class II odorant receptor.
Sci Adv, 12:eaeb9026-eaeb9026, 2026

PubMed Abstract: Mammalian odorant receptors (ORs) sense diverse environmental chemicals, yet structural insights into odorant recognition by mammalian class II ORs remain limited. Here, we present the cryo-EM structure of a native mammalian class II OR, mouse Olfr412, a human OR1D2 ortholog, bound to the odorant methyl--cinnamate and the G protein. The odorant-binding pocket of Olfr412 is located deeper within the transmembrane domain than that of the class I OR OR51E2 and is largely composed of poorly conserved hydrophobic residues, providing a structural basis for broad odorant recognition in class II ORs. Structural and molecular dynamics analyses suggest that the conserved Y plays a key role in odorant recognition and activation, functionally paralleling R in class I ORs and is further stabilized by intramolecular interaction with the conserved ECL2 residue E. Together, our findings uncover structural mechanisms underlying odorant recognition and activation in class II ORs.

PubMed: 41894497
DOI: 10.1126/sciadv.aeb9026

Experimental method

ELECTRON MICROSCOPY (3.2 Å)