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J. Biol. Chem., Vol. 279, Issue 6, 4459-4464, February 6, 2004

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Sulfur Single-wavelength Anomalous Diffraction Crystal Structure of a Pheromone-Binding Protein from the Honeybee Apis mellifera L^*

Audrey Lartigue, Arnaud Gruez, Loïc Briand¶, Florence Blon¶, Valérie Bézirard¶, Martin Walsh||, Jean-Claude Pernollet¶, Mariella Tegoni, and Christian Cambillau**

From the Architecture et Fonction des Macromolécules Biologiques, Unite Mixte de Recherche 6098 CNRS and Universités Aix-Marseille I and II, 13402 Marseille Cedex 20, France, ^¶Biochimie et Structure des Protéines, Unité de Recherches Institut National de la Recherche Agronomique 477, Domaine de Vilvert, F-78352 Jouy-en-Josas Cedex, France, and ^||Medical Research Council France, European Synchrotron Radiation Facility, B. P. 220, F-38043 Grenoble Cedex, France

Pheromone binding proteins (PBPs) are small helical proteins (13-17 kDa) present in several sensory organs from moth and other insect species. They are involved in the transport of pheromones from the sensillar lymph to the olfactory receptors. We report here the crystal structure of a PBP (Amel-ASP1) originating from the honey-bee (Apis mellifera) antennae and expressed as recombinant protein in the yeast Pichia pastoris. Crystals of Amel-ASP1 were obtained at pH 5.5 using the nano-drops technique of crystallization with a novel optimization procedure, and the structure was solved initially with the single-wavelength anomalous diffraction technique using sulfur anomalous dispersion. The structure of Amel-ASP1 has been refined at 1.6-Å resolution. Its fold is roughly similar to that of other PBP/odorant binding proteins, presenting six helices and three disulfide bridges. Contrary to the PBPs from Bombyx mori (Sandler, B. H., Nikonova, L., Leal, W. S., and Clardy, J. (2000) Chem. Biol. 7, 143-151) and Leucophea maderae (Lartigue, A., Gruez, A., Spinelli, S., Riviere, S., Brossut, R., Tegoni, M., and Cambillau, C. (2003) J. Biol. Chem. 278, 30213-30218), the extended C terminus folds into the protein and forms a wall of the internal hydrophobic cavity. Its backbone groups establish two hydrogen bonds with a serendipitous ligand, n-butyl-benzene-sulfonamide, an additive used in plastics. This mode of binding might, however, mimic that used by one of the pheromonal blend components and illustrates the binding versatility of PBPs.

Received for publication, October 13, 2003 , and in revised form, October 31, 2003.

The atomic coordinates and structure factors (code 1R5R) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This study was supported in part by the Conseil Général des Bouches-du-Rhone and by the Genopôles program.

A recipient of PACA region PhD Grant 9811/2177. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^** To whom correspondence should be addressed. Tel.: 33-49116-4501; Fax: 33-49116-4536; E-mail: cambillau{at}afmb.cnrs-mrs.fr.

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