1P28
The crystal structure of a pheromone binding protein from the cockroach Leucophaea maderae in complex with a component of the pheromonal blend: 3-hydroxy-butan-2-one.
Summary for 1P28
| Entry DOI | 10.2210/pdb1p28/pdb |
| Related | 1ORG 1OW4 |
| Descriptor | pheromone binding protein, S,3-HYDROXYBUTAN-2-ONE, R,3-HYDROXYBUTAN-2-ONE, ... (4 entities in total) |
| Functional Keywords | pheromone binding protein, 3-hydroxy-butan-2-one, transport protein |
| Biological source | Leucophaea maderae (Madeira cockroach) |
| Total number of polymer chains | 2 |
| Total formula weight | 28670.42 |
| Authors | Lartigue, A.,Gruez, A.,Spinelli, S.,Riviere, S.,Brossut, R.,Tegoni, M.,Cambillau, C. (deposition date: 2003-04-15, release date: 2003-08-05, Last modification date: 2024-10-30) |
| Primary citation | Lartigue, A.,Gruez, A.,Spinelli, S.,Riviere, S.,Brossut, R.,Tegoni, M.,Cambillau, C. THE CRYSTAL STRUCTURE OF A COCKROACH PHEROMONE-BINDING PROTEIN SUGGESTS A NEW LIGAND BINDING AND RELEASE MECHANISM J.Biol.Chem., 278:30213-30218, 2003 Cited by PubMed Abstract: Pheromone-binding proteins (PBPs) are small helical proteins found in sensorial organs, particularly in the antennae, of moth and other insect species. They were proposed to solubilize and carry the hydrophobic pheromonal compounds through the antennal lymph to receptors, participating thus in the peri-receptor events of signal transduction. The x-ray structure of Bombyx mori PBP (BmorPBP), from male antennae, revealed a six-helix fold forming a cavity that contains the pheromone bombykol. We have identified a PBP (LmaPBP) from the cockroach Leucophaea maderae in the antennae of the females, the gender attracted by pheromones in this species. Here we report the crystal structure of LmaPBP alone or in complex with a fluorescent reporter (amino-naphthalen sulfonate, ANS) or with a component of the pheromonal blend, 3-hydroxy-butan-2-one. Both compounds bind in the internal cavity of LmaPBP, which is more hydrophilic than BmorPBP cavity. LmaPBP structure ends just after the sixth helix (helix F). BmorPBP structure extends beyond the sixth helix with a stretch of residues elongated at neutral pH and folding as a seventh internalized helix at low pH. These differences between LmaPBP and BmorPBP structures suggest that different binding and release mechanism may be adapted to the hydrophilicity or hydrophobicity of the pheromonal ligand. PubMed: 12766173DOI: 10.1074/jbc.M304688200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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