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J. Biol. Chem., Vol. 278, Issue 44, 43728-43735, October 31, 2003
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**
From the
Laboratoire pour l'Utilisation du Rayonnement Electromagnétique, CNRS, CEA, MdR, BP. 34, 91898 Orsay Cedex, France and the
Institut de Génétique et Microbiologie, Bâtiment 360, Centre Scientifique Paris-Sud, 91405 Orsay Cedex, France
We have determined the crystal structure of YodA, an Escherichia coli protein of unknown function. YodA had been identified under conditions of cadmium stress, and we confirm that it binds metals such as cadmium and zinc. We have also found nickel bound in one of the crystal forms. YodA is composed of two domains: a main lipocalin/calycin-like domain and a helical domain. The principal metal-binding site lies on one side of the calycin domain, thus making YodA the first metal-binding lipocalin known. Our experiments suggest that YodA expression may be part of a more general stress response. From sequence analogy with the C-terminal domain of a metal-binding receptor of a member of bacterial ATP-binding cassette transporters, we propose a three-dimensional model for this receptor and suggest that YodA may have a receptor-type partner in E. coli.
Received for publication, April 29, 2003 , and in revised form, July 30, 2003.
The atomic coordinates and structure factors (code 1OEK
* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
¶ Present address: Ecole Polytechnique Fédérale, 1015 Lausanne, Switzerland.
|| Present address: Laboratoire de Biométrie et Biologie Evolutive, Bât. 711, Université Lyon 1, 43 blvd. 11 Novembre 1918, 69622 Villeurbanne Cedex, France.
** To whom correspondence should be addressed. Tel.: 33-1-64468050; Fax: 33-1-64464148; E-mail: Anita.Bentley{at}lure.u-psud.fr.
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