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'''Crystal Structure of B-form Bombyx mori Pheromone Binding Protein''' | '''Crystal Structure of B-form Bombyx mori Pheromone Binding Protein''' | ||
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[[Category: Lautenschlager, C.]] | [[Category: Lautenschlager, C.]] | ||
[[Category: Leal, W S.]] | [[Category: Leal, W S.]] | ||
[[Category: | [[Category: Alpha helical]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:59:12 2008'' | |||
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Revision as of 00:59, 4 May 2008
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 Sun May 4 03:59:12 2008
