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Originally published In Press as doi:10.1074/jbc.M009988200 on February 9, 2001

J. Biol. Chem., Vol. 276, Issue 19, 16328-16334, May 11, 2001
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The Crystal Structures of Apo and Complexed Saccharomyces cerevisiae GNA1 Shed Light on the Catalytic Mechanism of an Amino-sugar N-Acetyltransferase*

Caroline PeneffDagger §, Dominique Mengin-Lecreulx, and Yves BourneDagger ||

From the Dagger  UMR 6098 CNRS, 31 chemin Joseph Aiguier, 13402 Marseille Cedex 20, France and  UMR 8619 CNRS, Université Paris-Sud, Bâtiment 430, 91405 Orsay Cedex, France

The yeast enzymes involved in UDP-GlcNAc biosynthesis are potential targets for antifungal agents. GNA1, a novel member of the Gcn5-related N-acetyltransferase (GNAT) superfamily, participates in UDP-GlcNAc biosynthesis by catalyzing the formation of GlcNAc6P from AcCoA and GlcN6P. We have solved three crystal structures corresponding to the apo Saccharomyces cerevisiae GNA1, the GNA1-AcCoA, and the GNA1-CoA-GlcNAc6P complexes and have refined them to 2.4, 1.3, and 1.8 Å resolution, respectively. These structures not only reveal a stable, beta -intertwined, dimeric assembly with the GlcNAc6P binding site located at the dimer interface but also shed light on the catalytic machinery of GNA1 at an atomic level. Hence, they broaden our understanding of structural features required for GNAT activity, provide structural details for related aminoglycoside N-acetyltransferases, and highlight the adaptability of the GNAT superfamily members to acquire various specificities.

* This work was supported by grants from the CNRS to UMR 6098 (Marseille, Y. B.) and to UMR 8619 (Orsay, D.  M.-L.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The atomic coordinates and the structure factors (code 1I21, 1I12, and 1I1D) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

§ Holder of a CNRS Ph.D. fellowship.

|| To whom correspondence should be addressed. Tel.: +33-4-91-16-45-08; Fax: +33-4-91-16-45-36; E-mail: yves@afmb.cnrs-mrs.fr.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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