Extended Data Fig. 10. A potential route for coupling of odorant binding to pore opening and details of pore opening in the DEET-bound MhOR5 structure.

a, Top view of MhOR5 with helices represented as tubes in apo structure (blue) and eugenol-bound structure (pink). b, Close-up view of one subunit of the apo (blue, top) and eugenol-bound (pink, bottom) structures of MhOR5. Residues Leu465 (in S7b), Tyr362 (in S5) and Tyr380 (in S6, lining the binding pocket) and eugenol are shown as sticks with a translucent outline of the sphere representation. c, Mutation of Leu465 in S7 and Tyr362 in S5 into alanine impairs receptor function. A conservative substitution of Tyr362 to phenylalanine restores wild-type activity, highlighting the potential role of hydrophobic packing in connecting odorant binding with pore opening (n = 6). Dose–response curves represent the average across experiments, error bars denote s.e.m. Summary table of receptor data is in Supplementary Table 2. d, The lumen of the central pathway and side exits of the DEET-bound structure of MhOR5. e, Diameter of the ion pathway beginning at the extracellular membrane (position 0) and following the ion conduction pathway (solid line) and the central four-fold axis through the anchor domain (dashed line), calculated with HOLE. Blue line represents apo structure, pink line represents eugenol-bound structure and cyan line represents DEET-bound structure. f, Top view of the DEET-bound structure with inset (right) highlighting the positions of residues Gln467 and Val468.