Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractSingle-cell profiling screen identifies microtubule-dependent reduction of variability in signaling    Next AbstractQueen bee pheromone binding protein pH-induced domain swapping favors pheromone release »

J Mol Biol


Title:Structural basis of the honey bee PBP pheromone and pH-induced conformational change
Author(s):Pesenti ME; Spinelli S; Bezirard V; Briand L; Pernollet JC; Tegoni M; Cambillau C;
Address:"Architecture et Fonction des Macromolecules Biologiques, UMR 6098 CNRS and Universites de Marseille, Marseille, France"
Journal Title:J Mol Biol
Year:2008
Volume:20080427
Issue:1
Page Number:158 - 169
DOI: 10.1016/j.jmb.2008.04.048
ISSN/ISBN:1089-8638 (Electronic) 0022-2836 (Linking)
Abstract:"The behavior of insects and their perception of their surroundings are driven, in a large part, by odorants and pheromones. This is especially true for social insects, such as the honey bee, where the queen controls the development and the caste status of the other individuals. Pheromone perception is a complex phenomenon relying on a cascade of recognition events, initiated in antennae by pheromone recognition by a pheromone-binding protein and finishing with signal transduction at the axon membrane level. With to the objective of deciphering this initial step, we have determined the structures of the bee antennal pheromone-binding protein (ASP1) in the apo form and in complex with the main component of the queen mandibular pheromonal mixture, 9-keto-2(E)-decenoic acid (9-ODA) and with nonpheromonal components. In the apo protein, the C terminus obstructs the binding site. In contrast, ASP1 complexes have different open conformations, depending on the ligand shape, leading to different volumes of the binding cavity. The binding site integrity depends on the C terminus (111-119) conformation, which involves the interplay of two factors; i.e. the presence of a ligand and a low pH. Ligand binding to ASP1 is favored by low pH, opposite to what is observed with other pheromone-binding proteins, such as those of Bombyx mori and Anopheles gambiae"
Keywords:"Amino Acid Sequence Animals Apoproteins/chemistry Bees/*chemistry Carrier Proteins/*chemistry Fatty Acids, Monounsaturated/chemistry Hydrogen-Ion Concentration Insect Proteins/*chemistry Ligands Models, Molecular Molecular Sequence Data Palmitic Acid/chem;"
Notes:"MedlinePesenti, Marion E Spinelli, Silvia Bezirard, Valerie Briand, Loic Pernollet, Jean-Claude Tegoni, Mariella Cambillau, Christian eng Research Support, Non-U.S. Gov't Netherlands 2008/05/30 J Mol Biol. 2008 Jun 27; 380(1):158-69. doi: 10.1016/j.jmb.2008.04.048. Epub 2008 Apr 27"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 21-09-2024