2FJY

Crystal Structure of B-form Bombyx mori Pheromone Binding Protein

2FJY の概要

• エントリーDOI: 10.2210/pdb2fjy/pdb
• 分子名称: Pheromone-binding protein (2 entities in total)
• 機能のキーワード: alpha helical, transport protein
• 由来する生物種: Bombyx mori (domestic silkworm)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31806.28

構造登録者

Lautenschlager, C.,Leal, W.S.,Clardy, J. (登録日: 2006-01-03, 公開日: 2006-01-17, 最終更新日: 2024-10-09)

主引用文献

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

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: 16111659
DOI: 10.1016/j.bbrc.2005.07.176

実験手法

X-RAY DIFFRACTION (2.3 Å)