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Nucleic Acids Research Advance Access originally published online on April 10, 2007
Nucleic Acids Research 2007 35(8):2705-2718; doi:10.1093/nar/gkm162
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Nucleic Acids Research, 2007, Vol. 35, No. 8 2705-2718
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Structural Biology

Novel DNA-binding element within the C-terminal extension of the nuclear receptor DNA-binding domain

Michal Jakób1, Robert Kolodziejczyk1, Marek Orlowski1, Szymon Krzywda2, Agnieszka Kowalska1, Joanna Dutko-Gwózdz1, Tomasz Gwózdz1, Marian Kochman1, Mariusz Jaskólski2,3 and Andrzej Ozyhar1,*

1Department of Biochemistry, Faculty of Chemistry, Wroclaw University of Technology, Wybrzeze Wyspianskiego 27, 50-370 Wroclaw, Poland, 2Department of Crystallography, Faculty of Chemistry, A. Mickiewicz University, Poznan, Poland and 3Center for Biocrystallographic Research, Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland

*To whom correspondence should be addressed. Tel: +48-71-320-6333; Fax: +48-71-320-6337; Email: andrzej.ozyhar{at}pwr.wroc.pl

Received January 10, 2007. Revised March 2, 2007. Accepted March 5, 2007.

The heterodimer of the ecdysone receptor (EcR) and ultraspiracle (Usp), members of the nuclear receptors superfamily, is considered as the functional receptor for ecdysteroids initiating molting and metamorphosis in insects. Here we report the 1.95 Å structure of the complex formed by the DNA-binding domains (DBDs) the EcR and the Usp, bound to the natural pseudopalindromic response element. Comparison of the structure with that obtained previously, using an idealized response element, shows how the EcRDBD, which has been previously reported to possess extraordinary flexibility, accommodates DNA-induced structural changes. Part of the C-terminal extension (CTE) of the EcRDBD folds into an {alpha}-helix whose location in the minor groove does not match any of the locations previously observed for nuclear receptors. Mutational analyses suggest that the {alpha}-helix is a component of EcR-box, a novel element indispensable for DNA-binding and located within the nuclear receptor CTE. This element seems to be a general feature of all known EcRs.


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