1ORG

The crystal structure of a pheromone binding protein from the cockroach Leucophaea maderae reveals a new mechanism of pheromone binding

1ORG の概要

• エントリーDOI: 10.2210/pdb1org/pdb
• 関連するPDBエントリー: 1OW4 1P28
• 分子名称: pheromone binding protein, GLYCEROL (3 entities in total)
• 機能のキーワード: pheromone binding protein, apo-form, 6 alpha helix, transport protein
• 由来する生物種: Leucophaea maderae (Madeira cockroach)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26213.76

構造登録者

Lartigue, A.,Gruez, A.,Spinelli, S.,Riviere, S.,Brossut, R.,Tegoni, M.,Cambillau, C. (登録日: 2003-03-13, 公開日: 2003-08-05, 最終更新日: 2024-11-06)

主引用文献

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

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: 12766173
DOI: 10.1074/jbc.M304688200

実験手法

X-RAY DIFFRACTION (1.7 Å)