3ogn

Crystal Structure of an Odorant-binding Protein from the Southern House Mosquito Complexed with an Oviposition Pheromone

spinqualitylabelsall models 3ogn, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ogn is a 2 chain structure with sequence from Culex quinquefasciatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.3Å Ligands: 3OG, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8T6I2_CULQU Publication Abstract from PubMed Culex mosquitoes introduce the pathogens responsible for filariasis, West Nile virus, St. Louis encephalitis, and other diseases into humans. Currently, traps baited with oviposition semiochemicals play an important role in detection efforts and could provide an environmentally friendly approach to controlling their populations. The odorant binding proteins (OBPs) in the female's antenna play a crucial, if yet imperfectly understood, role in sensing oviposition cues. Here, we report the X-ray crystallography and NMR 3D structures of OBP1 for Culex quinquefasciatus (CquiOBP1) bound to an oviposition pheromone (5R,6S)-6-acetoxy-5-hexadecanolide (MOP). In both studies, CquiOBP1 had the same overall six-helix structure seen in other insect OBPs, but a detailed analysis revealed an important previously undescribed feature. There are two models for OBP-mediated signal transduction: (i) direct release of the pheromone from an internal binding pocket in a pH-dependent fashion and (ii) detection of a pheromone-induced conformational change in the OBP.pheromone complex. Although CquiOBP1 binds MOP in a pH-dependent fashion, it lacks the C terminus required for the pH-dependent release model. This study shows that CquiOBP binds MOP in an unprecedented fashion using both a small central cavity for the lactone head group and a long hydrophobic channel for its tail. Crystal and solution structures of an odorant-binding protein from the southern house mosquito complexed with an oviposition pheromone.,Mao Y, Xu X, Xu W, Ishida Y, Leal WS, Ames JB, Clardy J Proc Natl Acad Sci U S A. 2010 Oct 18. PMID:20956299 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Odorant binding protein 3D structures

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