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« Previous AbstractThe crystal structure of a cockroach pheromone-binding protein suggests a new ligand binding and release mechanism    Next AbstractExperimental manipulation of floral scent bouquets restructures flower-visitor interactions in the field »

Acta Crystallogr D Biol Crystallogr


Title:Crystallization and preliminary crystallographic study of a pheromone-binding protein from the cockroach Leucophaea maderae
Author(s):Lartigue A; Riviere S; Brossut R; Tegoni M; Cambillau C;
Address:"Architecture et Fonction des Macromolecules Biologiques, UMR 6098 CNRS and Universites Aix-Marseille I and 2, 31 Chemin Joseph Aiguier, 13402 Marseille CEDEX 20, France"
Journal Title:Acta Crystallogr D Biol Crystallogr
Year:2003
Volume:20030425
Issue:Pt 5
Page Number:916 - 918
DOI: 10.1107/s0907444903004116
ISSN/ISBN:0907-4449 (Print) 0907-4449 (Linking)
Abstract:"Pheromone-binding proteins (PBPs) are small helical proteins (13-18 kDa) present in various sensory organs of moths and other insect species. An antennal protein from the cockroach Leucophaea maderae (LmaPBP) has been found to share all the hallmarks of the PBP family and is expressed specifically in the female adult antennae, the gender that perceives the sex pheromone. Here, the crystallization of LmaPBP expressed as a recombinant protein in Escherichia coli periplasm is reported. Crystals of LmaPBP were obtained by the sitting-drop vapour-diffusion method using a nanodrop-dispensing robot. The protein crystallizes in two different crystal forms. Form 1 belongs to space group P1, with unit-cell parameters a = 43.2, b = 45.1, c = 45.7 A, alpha = 118.6, beta = 93.0, gamma = 106.9 degrees. With two molecules in the asymmetric unit, V(M) is 2.7 A(3) Da(-1) and the solvent content is 47%. A complete data set has been collected at 1.6 A resolution on beamline ID14-2 (ESRF, Grenoble). Form 2 was obtained in the presence of the pheromone (3-hydroxy-butan-2-one) and belongs to space group P2(1), with unit-cell parameters a = 38.2, b = 62.2, c = 45.1 A, beta = 93.0 degrees. With two molecules in the asymmetric unit, V(M) is 2.0 A(3) Da(-1) and the solvent content is 39%. A complete data set has been collected at 1.7 A resolution on beamline BM14 (ESRF, Grenoble). SeMet expression has been performed with a view to solving the structure by MAD data collection using the Se absorption edge"
Keywords:"Amino Acid Sequence Animals Carrier Proteins/biosynthesis/*chemistry/genetics Cockroaches/*chemistry Crystallization/methods Crystallography, X-Ray Female *Insect Proteins Molecular Sequence Data Recombinant Proteins/biosynthesis/chemistry/genetics Sequen;"
Notes:"MedlineLartigue, Audrey Riviere, Stephane Brossut, Remy Tegoni, Mariella Cambillau, Christian eng Research Support, Non-U.S. Gov't 2003/06/05 Acta Crystallogr D Biol Crystallogr. 2003 May; 59(Pt 5):916-8. doi: 10.1107/s0907444903004116. Epub 2003 Apr 25"

 
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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.
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