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Biochem Biophys Res Commun. 2014 Apr 18;446(4):1042-6. doi: 10.1016/j.bbrc.2014.03.054. Epub 2014 Mar 21.

Insights into structural features determining odorant affinities to honey bee odorant binding protein 14.

Author information

1
Austrian Institute of Technology GmbH, AIT, Donau-City Str. 1, 1220 Vienna, Austria.
2
Institute of Molecular Modeling and Simulation, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
3
Center of Electrochemical Surface Technology, CEST, Viktor-Kaplan-Straße 2, 2700 Wiener Neustadt, Austria.
4
Institut für Biologische Chemie, Universität Wien, Währinger Straße 38, 1090 Wien, Austria.
5
Department of Agriculture, Food and Environment, University of Pisa, Via del Borghetto 80, 56124 Pisa, Italy.
6
Austrian Institute of Technology GmbH, AIT, Donau-City Str. 1, 1220 Vienna, Austria; Center of Electrochemical Surface Technology, CEST, Viktor-Kaplan-Straße 2, 2700 Wiener Neustadt, Austria. Electronic address: c.nowak@ait.ac.at.
7
Austrian Institute of Technology GmbH, AIT, Donau-City Str. 1, 1220 Vienna, Austria. Electronic address: Melanie.Larisika@ait.ac.at.

Abstract

Molecular interactions between odorants and odorant binding proteins (OBPs) are of major importance for understanding the principles of selectivity of OBPs towards the wide range of semiochemicals. It is largely unknown on a structural basis, how an OBP binds and discriminates between odorant molecules. Here we examine this aspect in greater detail by comparing the C-minus OBP14 of the honey bee (Apis mellifera L.) to a mutant form of the protein that comprises the third disulfide bond lacking in C-minus OBPs. Affinities of structurally analogous odorants featuring an aromatic phenol group with different side chains were assessed based on changes of the thermal stability of the protein upon odorant binding monitored by circular dichroism spectroscopy. Our results indicate a tendency that odorants show higher affinity to the wild-type OBP suggesting that the introduced rigidity in the mutant protein has a negative effect on odorant binding. Furthermore, we show that OBP14 stability is very sensitive to the position and type of functional groups in the odorant.

KEYWORDS:

Circular dichroism; Ligand binding; Molecular dynamics; Odorant binding protein; Thermal stability

PMID:
24661875
DOI:
10.1016/j.bbrc.2014.03.054
[Indexed for MEDLINE]
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