6QQ4

Odorant-binding protein dmelOBP28a from Drosophila melanogaster

6QQ4 の概要

• エントリーDOI: 10.2210/pdb6qq4/pdb
• 分子名称: General odorant-binding protein 28a, PENTAETHYLENE GLYCOL, MALONIC ACID, ... (4 entities in total)
• 機能のキーワード: odorant-binding protein, pheromone-binding protein, drosophila melanogaster, olfaction, gustation, taste, transport, carrier, perireceptor events, complex, transport protein
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26123.68

構造登録者

Gonzalez, D.,Neiers, F.,Gotthard, G.,Briand, L. (登録日: 2019-02-17, 公開日: 2020-03-18, 最終更新日: 2024-10-09)

主引用文献

Gonzalez, D.,Rihani, K.,Neiers, F.,Poirier, N.,Fraichard, S.,Gotthard, G.,Chertemps, T.,Maibeche, M.,Ferveur, J.F.,Briand, L.
The Drosophila odorant-binding protein 28a is involved in the detection of the floral odour ss-ionone.
Cell.Mol.Life Sci., 77:2565-2577, 2020

PubMed Abstract: Odorant-binding proteins (OBPs) are small soluble proteins that are thought to transport hydrophobic odorants across the aqueous sensillar lymph to olfactory receptors. A recent study revealed that OBP28a, one of the most abundant Drosophila OBPs, is not required for odorant transport, but acts in buffering rapid odour variation in the odorant environment. To further unravel and decipher its functional role, we expressed recombinant OBP28a and characterized its binding specificity. Using a fluorescent binding assay, we found that OBP28a binds a restricted number of floral-like chemicals, including ß-ionone, with an affinity in the micromolar range. We solved the X-ray crystal structure of OBP28a, which showed extensive conformation changes upon ligand binding. Mutant flies genetically deleted for the OBP28a gene showed altered responses to ß-ionone at a given concentration range, supporting its essential role in the detection of specific compounds present in the natural environment of the fly.

PubMed: 31564000
DOI: 10.1007/s00018-019-03300-4

実験手法

X-RAY DIFFRACTION (1.998 Å)