1KX9

ANTENNAL CHEMOSENSORY PROTEIN A6 FROM THE MOTH MAMESTRA BRASSICAE

1KX9 の概要

• エントリーDOI: 10.2210/pdb1kx9/pdb
• 関連するPDBエントリー: 1KX8
• 分子名称: CHEMOSENSORY PROTEIN A6, ACETATE ION (3 entities in total)
• 機能のキーワード: all helix, lipid transport
• 由来する生物種: Mamestra brassicae (cabbage moth)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26307.77

構造登録者

Lartigue, A.,Campanacci, V.,Roussel, A.,Larsson, A.M.,Jones, T.A.,Tegoni, M.,Cambillau, C. (登録日: 2002-01-31, 公開日: 2002-12-04, 最終更新日: 2024-10-30)

主引用文献

Lartigue, A.,Campanacci, V.,Roussel, A.,Larsson, A.M.,Jones, T.A.,Tegoni, M.,Cambillau, C.
X-ray structure and ligand binding study of a moth chemosensory protein
J.Biol.Chem., 277:32094-32098, 2002

PubMed Abstract: Chemosensory proteins (CSPs) are believed to be involved in chemical communication and perception. Such proteins, of M(r) 13,000, have been isolated from several sensory organs of a wide range of insect species. Several CSPs have been identified in the antennae and proboscis of the moth Mamestra brassicae. One of them, CSPMbraA6, a 112-amino acid antennal protein, has been expressed in large quantities and is soluble in the Escherichia coli periplasm. X-ray structure determination has been performed in parallel with ligand binding assays using tryptophan fluorescence quenching. The protein has overall dimensions of 25 x 30 x 32 A and exhibits a novel type of alpha-helical fold with six helices connected by alpha-alpha loops. A narrow channel extends within the protein hydrophobic core. Fluorescence quenching with brominated alkyl alcohols or fatty acids and modeling studies indicates that CSPMbraA6 is able to bind such compounds with C12-18 alkyl chains. These ubiquitous proteins might have the role of extracting hydrophobic linear compounds (pheromones, odors, or fatty acids) dispersed in the phospholipid membrane and transporting them to their receptor.

PubMed: 12068017
DOI: 10.1074/jbc.M204371200

実験手法

X-RAY DIFFRACTION (1.65 Å)