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J. Biol. Chem., Vol. 279, Issue 33, 34890-34897, August 13, 2004

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Crystal Structure and Functional Characterization of Yeast YLR011wp, an Enzyme with NAD(P)H-FMN and Ferric Iron Reductase Activities^*

Dominique Liger, Marc Graille¶, Cong-Zhao Zhou||, Nicolas Leulliot, Sophie Quevillon-Cheruel, Karine Blondeau**, Joël Janin¶, and Herman van Tilbeurgh¶

From the Institut de Biochimie et de Biophysique Moléculaire et Cellulaire (CNRS-Unité Mixte de Recherche (UMR) 8619), Université Paris-Sud, Bâtiment 430, 91405 Orsay, France, ^¶Laboratoire d'Enzymologie et Biochimie Structurales (CNRS-Unité Propre de Recherche 9063), Bâtiment 34, 1 Avenue de la Terrasse, 91198 Gif sur Yvette, France, and ^**Institut de Génétique et Microbiologie (CNRS-UMR 8621), Université Paris-Sud, Bâtiment 360, 91405 Orsay, France

Flavodoxins are involved in a variety of electron transfer reactions that are essential for life. Although FMN-binding proteins are well characterized in prokaryotic organisms, information is scarce for eukaryotic flavodoxins. We describe the 2.0-Å resolution crystal structure of the Saccharomyces cerevisiae YLR011w gene product, a predicted flavoprotein. YLR011wp indeed adopts a flavodoxin fold, binds the FMN cofactor, and self-associates as a homodimer. Despite the absence of the flavodoxin key fingerprint motif involved in FMN binding, YLR011wp binds this cofactor in a manner very analogous to classical flavodoxins. YLR011wp closest structural homologue is the homodimeric Bacillus subtilis Yhda protein (25% sequence identity) whose homodimer perfectly superimposes onto the YLR011wp one. Yhda, whose function is not documented, has 53% sequence identity with the Bacillus sp. OY1–2 azoreductase. We show that YLR011wp has an NAD(P)H-dependent FMN reductase and a strong ferricyanide reductase activity. We further demonstrate a weak but specific reductive activity on azo dyes and nitrocompounds.

Received for publication, May 14, 2004 , and in revised form, June 3, 2004.

The atomic coordinates and structure factors (code 1T0I) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work is supported in part by grants from the Ministère de la Recherche et de la Technologie (Programme Génopoles) and the Association pour la Recherche sur le Cancer (to M. G.). 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.

Both authors contributed equally to the work.

^|| Present address: School of Life Science, University of Science and Technology of China, Hefei Anhui 230027, People's Republic of China.

To whom correspondence should be addressed. Tel.: 33-1-69-82-34-91; Fax: 33-1-69-82-31-29; E-mail: herman{at}lebs.cnrs-gif.fr.

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