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Originally published In Press as doi:10.1074/jbc.M305725200 on July 7, 2003

J. Biol. Chem., Vol. 278, Issue 38, 36887-36896, September 19, 2003
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The Iodothyronine Selenodeiodinases Are Thioredoxin-fold Family Proteins Containing a Glycoside Hydrolase Clan GH-A-like Structure*

Isabelle Callebaut {ddagger}, Cyntia Curcio-Morelli §, Jean-P. Mornon {ddagger}, Balazs Gereben ¶ ||, Christoph Buettner §, Stephen Huang §, Bertrand Castro {ddagger} **, Tatiana L. Fonseca §, John W. Harney §, P. Reed Larsen § and Antonio C. Bianco § {ddagger}{ddagger}

From the {ddagger}Poôle Bio, Laboratoive de Minéralogie-Cristallographie de Paris, CNRS UMR7590, Universities Paris 6 and Paris 7, Paris 75252 Cedex 05, France, ||Department of Endocrine and Behavioral Neurobiology, Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest H-1083 Hungary, §Thyroid Section, Division of Endocrinology, Diabetes and Hypertension, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115, and **Sanofi-Synthelabo, 94255 Gentilly Cedex, France

The three iodothyronine selenodeiodinases catalyze the initiation and termination of thyroid hormone effects in vertebrates. Structural analyses of these proteins have been hindered by their integral membrane nature and the inefficient eukaryotic-specific pathway for selenoprotein synthesis. Hydrophobic cluster analysis used in combination with Position-specific Iterated BLAST reveals that their extramembrane portion belongs to the thioredoxin-fold superfamily for which experimental structure information exists. Moreover, a large deiodinase region imbedded in the thioredoxin fold shares strong similarities with the active site of iduronidase, a member of the clan GH-A-fold of glycoside hydrolases. This model can explain a number of results from previous mutagenesis analyses and permits new verifiable insights into the structural and functional properties of these enzymes.

Received for publication, June 2, 2003

* This work was supported by DK 36256 and DK58538 grants from the NIH. 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.

A Magyary Zoltán Postdoctoral Fellow of the Hungarian Education Ministry and supported by a Felsõoktatási Kutatási és Fejlesztési Pályázat (FKFP 0036/2001) grant and the Fifth EC Framework Program (QLG3 2000-00844).

{ddagger}{ddagger} To whom correspondence should be addressed: Brigham and Women's Hospital, 77 Avenue Louis Pasteur, HIM Bldg. 643, Boston, MA 02115. Tel.: 617-525-5153; Fax: 617-731-4718; E-mail: abianco{at}partners.org.


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