Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 107, Issue 44, Pages 19102-19107Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1012274107
Keywords
AaegOBP1; AgamOBP1; CquiOBP1; NMR; X-ray crystallography
Categories
Funding
- National Science Foundation [0918177]
- National Institutes of Health [CA024487, EY012347, NS059404]
- US Department of Agriculture-Agriculture and Food Research Institute [2010-65105-20582]
- Bedoukian Research, Inc
- NIFA [581000, 2010-65105-20582] Funding Source: Federal RePORTER
- Direct For Biological Sciences [0918177] Funding Source: National Science Foundation
- Division Of Integrative Organismal Systems [0918177] Funding Source: National Science Foundation
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Culex mosquitoes introduce the pathogens responsible for filariasis, West Nile virus, St. Louis encephalitis, and other diseases into humans. Currently, traps baited with oviposition semiochemicals play an important role in detection efforts and could provide an environmentally friendly approach to controlling their populations. The odorant binding proteins (OBPs) in the female's antenna play a crucial, if yet imperfectly understood, role in sensing oviposition cues. Here, we report the X-ray crystallography and NMR 3D structures of OBP1 for Culex quinquefasciatus (CquiOBP1) bound to an oviposition pheromone (5R,6S)-6-acetoxy-5-hexadecanolide (MOP). In both studies, CquiOBP1 had the same overall six-helix structure seen in other insect OBPs, but a detailed analysis revealed an important previously undescribed feature. There are two models for OBP-mediated signal transduction: (i) direct release of the pheromone from an internal binding pocket in a pH-dependent fashion and (ii) detection of a pheromone-induced conformational change in the OBP.pheromone complex. Although CquiOBP1 binds MOP in a pH-dependent fashion, it lacks the C terminus required for the pH-dependent release model. This study shows that CquiOBP binds MOP in an unprecedented fashion using both a small central cavity for the lactone head group and a long hydrophobic channel for its tail.
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