3fba Pheromone of Apis mellifera

Structure of Binding Pheromone in Apis MelliferaStructure of Binding Pheromone in Apis Mellifera

This is a default text for your page 3fba Pheromone of Apis mellifera. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia or to the article describing Jmol to the rescue. Background Bees are considered social insects, therefore their perception and behavior can be influenced by their environment through pheromones and particular odors. 3FBA is the Crystal structure of a pheromone binding protein from Apis mellifera in complex with the Queen mandibular pheromone (QMP). The perception of this structure is complex, as it relies on a cascade of recognition that is first sequenced by the antennae by a pheromone-binding protein that recognizes it and finished with a transduction signal at the axon membrane level. This particular pheromone serves as an anesthetic and paralyzes intruders and signals the worker bees to remove the intruder from the hive, swarming behavior, mating behavior, and suppresses ovary development in workers (making all females sterile except for the queen and a small portion of fertile males referred to as drones). Structure The 3FBA protein possesses an asymmetric configuration and the protein stoichiometry is to be seen as a monomer (the foundational structure that can be paired with another to form a larger molecule). The expression system in which the 3FBA operates is the Pichia pastoris. P. pastoris is a methylotroph yeast that is capable of growing with simple alcohol as the only energy source. High yields at a low cost help aid in 3FBA production. P. pastoris can do most post-translational modifications and the obtained recombinant proteins undergo protein folding, protein processing, glycosylation, and disulfide bond formation2. 3FBA undergoes transformation via a vector into the P. pastoris via electroporation. DNA expression and PCR are conducted to make sure the yeast, P. pastoris, uptook 3FBA. As stated above, there are many types of pheromones that honeybees operate from. The queen mandibular pheromone is one of the most important containing compounds such as semi-volatile carboxylic acids and aromatic compounds like the ligand 9ODA that stands for 9-oxo-2-decenoic acid more commonly referred to as the queen substance1. 3FBA structure features two types of ligands: 9OD and GOL. Structural highlights The 9ODA structure consists of 10 Carbons, 16 Hydrogens, and 3 Oxygens. The hydrocarbons present on the cuticle act as conserved queen signals. The other important ligand in 3FBA is GOL which stands for glycerol. The structure of glycerol, a small hydrophilic tri-alcohol molecule that features 3 Carbons, 8 Hydrogens, and 3 Oxygens. The binding site integrity depends on the C terminus (111-119) conformation, which involves the interplay of two factors--a low pH and a ligand. The ligand binding to 3FBA is favored by low pH, opposite to what is observed with other pheromone-binding proteins, such as those of Bombyx mori and Anopheles gambiae. Structural basis of the honey bee PBP pheromone and pH-induced conformational change.,Pesenti ME, Spinelli S, Bezirard V, Briand L, Pernollet JC, Tegoni M, Cambillau C J Mol Biol. 2008 Jun 27;380(1):158-69. Epub 2008 Apr 27. PMID:18508083 Structurally, 3FBA also features a Zinc ion that is utilized as a structural cofactor. Cofactors assist in catalytic activity or provide structural contributions to protein structure and/or confirmation. The residues that surround the Zinc ion and the binding site are most conserved in the 3FBA structure. Relevance The perception of this structure is complex, as it relies on a cascade of recognition that is first sequenced by the antennae by a pheromone-binding protein that recognizes it and finished with a transduction signal at the axon membrane level <PMID:1ref> spinqualitylabelsall models The Queen mandibular pheromone (QMP). The perception is complex, as it relies on a cascade of recognition that is first sequenced by the antennae by a pheromone-binding protein that recognizes it and finished with a transduction signal at the axon membrane level1 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

spinqualitylabelsall models The perception of this structure is complex, as it relies on a cascade of recognition that is first sequenced by the antennae by a pheromone-binding protein that recognizes it and finished with a transduction signal at the axon membrane level1 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

ReferencesReferences

Pesenti, Marion E., et al. “Structural Basis of the Honey Bee PBP Pheromone and PH-Induced Conformational Change.” Journal of Molecular Biology, Academic Press, 27 Apr. 2008, www.sciencedirect.com/science/article/abs/pii/S0022283608004944?via%3Dihub. Cereghino, G. P., Cereghino, J. L., Ilgen, C., Cregg, J. M. Production of recombinant proteins in fermenter cultures of the yeast Pichia pastoris. Curr Opin Biotechnol. 4, 329-332 (2002). “Queen Substance.” National Center for Biotechnology Information. PubChem Compound Database, U.S. National Library of Medicine, pubchem.ncbi.nlm.nih.gov/compound/Queen-substance#section=Information-Sources.