3D73

Crystal structure of a pheromone binding protein mutant D35A, from Apis mellifera, at pH 7.0

Summary for 3D73

• Entry DOI: 10.2210/pdb3d73/pdb
• Related: 2H8V 3BFA 3BFB 3BFH 3BJH 3CAB 3CDN 3CYZ 3CZ0 3CZ1 3CZ2 3D74 3D75 3D76 3D77 3D78
• Descriptor: Pheromone-binding protein ASP1, N-BUTYL-BENZENESULFONAMIDE (3 entities in total)
• Functional Keywords: pheromone binding protein, honey bee, apis mellifera, signal transduction, queen mandibular protein, ph
• Biological source: Apis mellifera (Honeybee)
• Total number of polymer chains: 2
• Total formula weight: 26941.45

Authors

Pesenti, M.E.,Spinelli, S.,Bezirard, V.,Briand, L.,Pernollet, J.C.,Tegoni, M.,Cambillau, C. (deposition date: 2008-05-20, release date: 2009-05-26, Last modification date: 2023-11-01)

Primary citation

Pesenti, M.E.,Spinelli, S.,Bezirard, V.,Briand, L.,Pernollet, J.C.,Campanacci, V.,Tegoni, M.,Cambillau, C.
Queen bee pheromone binding protein pH-induced domain swapping favors pheromone release
J.Mol.Biol., 390:981-990, 2009

PubMed Abstract: In honeybee (Apis mellifera) societies, the queen controls the development and the caste status of the members of the hive. Queen bees secrete pheromonal blends comprising 10 or more major and minor components, mainly hydrophobic. The major component, 9-keto-2(E)-decenoic acid (9-ODA), acts on the workers and male bees (drones), eliciting social or sexual responses. 9-ODA is captured in the antennal lymph and transported to the pheromone receptor(s) in the sensory neuron membranes by pheromone binding proteins (PBPs). A key issue is to understand how the pheromone, once tightly bound to its PBP, is released to activate the receptor. We report here on the structure at physiological pH of the main antennal PBP, ASP1, identified in workers and male honeybees, in its apo or complexed form, particularly with the main component of the queen mandibular pheromonal mixture (9-ODA). Contrary to the ASP1 structure at low pH, the ASP1 structure at pH 7.0 is a domain-swapped dimer with one or two ligands per monomer. This dimerization is disrupted by a unique residue mutation since Asp35 Asn and Asp35 Ala mutants remain monomeric at pH 7.0, as does native ASP1 at pH 4.0. Asp35 is conserved in only approximately 30% of medium-chain PBPs and is replaced by other residues, such as Asn, Ala and Ser, among others, thus excluding that they may perform domain swapping. Therefore, these different medium-chain PBPs, as well as PBPs from moths, very likely exhibit different mechanisms of ligand release or receptor recognition.

PubMed: 19481550
DOI: 10.1016/j.jmb.2009.05.067

Experimental method

X-RAY DIFFRACTION (2.03 Å)