Sulfur single-wavelength anomalous diffraction crystal structure of a pheromone-binding protein from the honeybee Apis mellifera L
| Autor: | Valérie Bézirard, Jean-Claude Pernollet, Loïc Briand, Audrey Lartigue, Florence Blon, Arnaud Gruez, Mariella Tegoni, Martin A. Walsh, Christian Cambillau |
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| Přispěvatelé: | Centre National de la Recherche Scientifique (CNRS), Biochimie bactérienne (BIOBAC), Institut National de la Recherche Agronomique (INRA), Medical Research Council France, Partenaires INRAE |
| Jazyk: | angličtina |
| Rok vydání: | 2004 |
| Předmět: |
Models
Molecular Protein Conformation Odorant binding Static Electricity Crystal structure Crystallography X-Ray Biochemistry Pichia pastoris apidae HONEYBEE 03 medical and health sciences 0302 clinical medicine Bombyx mori Animals Pheromone binding ODORANT BINDING PROTEIN phéromone récepteur odorant Molecular Biology odorant 030304 developmental biology 0303 health sciences biology Hydrogen bond C-terminus Cell Biology Bees biology.organism_classification PHEROMONE BINDING PROTEIN Recombinant Proteins [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM] INSECTE Crystallography Insect Proteins structure des protéines Carrier Proteins Crystallization Pheromone binding protein Sulfur 030217 neurology & neurosurgery |
| Zdroj: | Journal of Biological Chemistry 6 (279), 4459-4464. (2004) Journal of Biological Chemistry Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2004, 279 (6), pp.4459-4464. ⟨10.1074/jbc.M311212200⟩ |
| ISSN: | 0021-9258 1083-351X |
| DOI: | 10.1074/jbc.M311212200⟩ |
| Popis: | International audience; 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. |
| Databáze: | OpenAIRE |
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