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Sulfur single-wavelength anomalous diffraction crystal structure of a pheromone-binding protein from the honeybee Apis mellifera L. Inra
Lartigue, A.; Gruez, A.; Briand, L.; Blon, F.; Bezirard, V.; Walsh, M.; Pernollet, J.C.; Tegoni, M.; Cambillau, C..
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...
Tipo: Journal Article Palavras-chave: ODORANT; RECEPTEUR OLFACTIF; STRUCTURE DES PROTEINES ODORANT BINDING PROTEIN; PHEROMONE BINDING PROTEIN; HONEYBEE.
Ano: 2004 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2007c936945a&uri=/notices/prodinra1/2010/11/
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The insect attractant 1-Octen-3-o1 is the natural ligand of bovine odorant-binding protein Inra
Ramoni, R.; Vincent, F.; Grolli, S.; Conti, V.; Malosse, C.; Boyer, F.D.; Nagnan-Le Meillour, P.; Spinelli, S.; Cambillau, C.; Tegoni, M..
Bovine odorant-binding protein (bOBP) is a dimeric lipocalin present in large amounts in the respiratory and olfactory nasal mucosa. The structure of bOBP refined at 2.0-Å resolution revealed an elongated volume of electron density inside each buried cavity, indicating the presence of one (or several) naturally occurring copurified ligand(s) (Tegoni et al. (1996)Nat. Struct. Biol. 3, 863–867; Bianchet et al.(1996) Nat. Struct. Biol. 3, 934–939). In the present work, by combining mass spectrometry, x-ray crystallography (1.8-Å resolution), and fluorescence, it has been unambiguously established that natural bOBP contains the racemic form of 1-octen-3-ol. This volatile substance is a typical component of bovine breath and in general of odorous body...
Tipo: Journal Article Palavras-chave: TECHNIQUE ANALYTIQUE; SPECTROMÉTRIE DE MASSE; CHROMATOGRAPHIE EN PHASE GAZEUSE; STRUCTURE TRIDIMENSIONNELLE; LIGAND FLUORESCENCE SPECTROSCOPY; URINARY PROTEINS; NASAL-MUCOSA; AFFINITIES; MECHANISM; LIPOCALIN; MOSQUITOS; RECEPTOR.
Ano: 2001 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0200012319094103&uri=/notices/prodinra1/2010/10/
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