期刊
PLOS ONE
卷 8, 期 2, 页码 -出版社
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pone.0053840
关键词
-
资金
- Agriculture and Food Research Initiative Competitive Grant from the USDA National Institute of Food and Agriculture [2010-65105-20582]
- National Science Foundation [0918177]
- National Institutes of Health [1R01AI095514-01A1]
- National Research Foundation of Korea [2010-010837]
- Kyungpook National University [2010-05950000]
- NIFA [581000, 2010-65105-20582] Funding Source: Federal RePORTER
- Grants-in-Aid for Scientific Research [23580070] Funding Source: KAKEN
The navel orangeworm, Amyelois transitella is a major agricultural pest causing large losses in a variety of tree crops. Control of this insect pest may be achieved by interfering with olfactory pathways to block detection of female-produced sex pheromones and consequently, disrupt mating. The first component of this pathway is the pheromone-binding protein AtraPBP1, which recognizes the pheromone and presents it to the odorant receptor housed in a sensory neuron of the male antennae. Release of the ligand depends on a pH-induced conformational change associated with the acidity of the membrane surface. To characterize this conformational change and to understand how pheromones bind, we have determined the high resolution crystal structures of AtraPBP1 in complex with two main constituents of the sex pheromone, i.e., (11Z, 13Z)-hexadecadienal and (11Z, 13Z)-hexadecadienol. Comparison with the structure of the unliganded form demonstrates a large similar to 90 degrees movement of the C-terminal helix which is observed in other pheromone- or odorant-binding proteins accompanied by an unpredicted 37 degrees displacement of the N-terminal helix. Molecular dynamic trajectories suggest that the conformational change of the alpha 1 helix facilitates the movement of the C-terminal helix.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据