2FJY
Crystal Structure of B-form Bombyx mori Pheromone Binding Protein
Summary for 2FJY
| Entry DOI | 10.2210/pdb2fjy/pdb |
| Descriptor | Pheromone-binding protein (2 entities in total) |
| Functional Keywords | alpha helical, transport protein |
| Biological source | Bombyx mori (domestic silkworm) |
| Total number of polymer chains | 2 |
| Total formula weight | 31806.28 |
| Authors | Lautenschlager, C.,Leal, W.S.,Clardy, J. (deposition date: 2006-01-03, release date: 2006-01-17, Last modification date: 2024-10-09) |
| Primary citation | Lautenschlager, C.,Leal, W.S.,Clardy, J. Coil-to-helix transition and ligand release of Bombyx mori pheromone-binding protein. Biochem.Biophys.Res.Commun., 335:1044-1050, 2005 Cited by PubMed Abstract: The transport of hydrophobic insect pheromones through the aqueous medium surrounding their receptors is assisted by pheromone-binding proteins (PBPs). The protein from the silkworm moth Bombyx mori, BmorPBP, exhibits a pH-dependent conformational change postulated to trigger the release of the pheromone bombykol to its receptor. At low pH, an alpha-helix occupies the same binding pocket that houses the pheromone in the BmorPBP-bombykol complex at high pH. We have determined the crystal structure of apo BmorPBP at a resolution of 2.3 angstroms and pH 7.5, which has surprisingly a structure similar to the A-form. These data suggest that BmorPBP undergoes a ligand-dependent conformational change in addition to the previously described pH-dependent conformational change. Analysis of the alpha-helix occupying the binding pocket reveals an amphipathic helix with three acidic residues along one face that are conserved among lepidopteran PBPs and may be involved in a conformational transition of BmorPBP at the receptor membrane. PubMed: 16111659DOI: 10.1016/j.bbrc.2005.07.176 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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