3r1p

Odorant Binding Protein 7 from Anopheles gambiae with Four Disulfide Bridges, form P1

spinqualitylabelsall models 3r1p, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3r1p is a 6 chain structure with sequence from Anopheles gambiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.85Å Ligands: PLM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q7PXT9_ANOGA Publication Abstract from PubMed Anopheles gambiae (Agam) targets human and animals by using its olfactory system, leading to the spread of Plasmodium falciparum, the malaria vector. Odorant binding proteins (OBPs) participate to the first event in odorant recognition and constitute an interesting target for insect control. OBPs interact with olfactory receptors to which they deliver the odorant molecule. We have undertaken a large-scale study of proteins belonging to the olfactory system of Agam with in mind of designing strong olfactory repellants. Here, we report the expression, three-dimensional structures and binding properties of AgamOBP07, a member of a new structural class of OBPs, characterized by the occurrence of eight cysteines. We showed that AgamOBP07 possesses seven alpha-helices and four disulfide bridges, instead of six alpha-helices and three disulfide bridges in classical OBPs. The extra seventh helix is located at the surface of the protein, locked by the fourth disulfide bridge, and forms a wall of the internal cavity. The binding site of the protein is mainly hydrophobic, elongated and open and is able to accommodate elongated ligands, linear or polycyclic, as suggested also by binding experiments. An elongated electron density was observed in the internal cavity of the purified protein, belonging to a serendipitous ligand. The structure of AgamOBP07 in complex with an azo-bicyclic model compound reveals that a large conformational change in the protein has reshaped its binding site, provoking helix 4 unfolding and doubling of the cavity volume. The Crystal Structure of Odorant Binding Protein 7 from Anopheles gambiae Exhibits an Outstanding Adaptability of Its Binding Site.,Lagarde A, Spinelli S, Tegoni M, He X, Field L, Zhou JJ, Cambillau C J Mol Biol. 2011 Oct 12. PMID:22019737 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Odorant binding protein 3D structures

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