2fjy
From Proteopedia
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Crystal Structure of B-form Bombyx mori Pheromone Binding Protein
Overview
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.
About this Structure
2FJY is a Single protein structure of sequence from Bombyx mori. Full crystallographic information is available from OCA.
Reference
Coil-to-helix transition and ligand release of Bombyx mori pheromone-binding protein., Lautenschlager C, Leal WS, Clardy J, Biochem Biophys Res Commun. 2005 Oct 7;335(4):1044-50. PMID:16111659
Page seeded by OCA on Wed Nov 21 10:35:49 2007
