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Originally published In Press as doi:10.1074/jbc.M011225200 on December 15, 2000

J. Biol. Chem., Vol. 276, Issue 15, 11844-11851, April 13, 2001
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Crystal Structure of Streptococcus pneumoniae N-Acetylglucosamine-1-phosphate Uridyltransferase Bound to Acetyl-coenzyme A Reveals a Novel Active Site Architecture*

Gerlind SulzenbacherDagger §, Laurent GalDagger , Caroline PeneffDagger , Florence Fassy||, and Yves BourneDagger **

From the Dagger  AFMB-UMR6098, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France and || Aventis Pharma-Hoechst Marion Roussel, Infectious Diseases Group, 102 Route de Noisy, 93235 Romainville Cedex, France

The bifunctional bacterial enzyme N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU) catalyzes the two-step formation of UDP-GlcNAc, a fundamental precursor in bacterial cell wall biosynthesis. With the emergence of new resistance mechanisms against beta -lactam and glycopeptide antibiotics, the biosynthetic pathway of UDP-GlcNAc represents an attractive target for drug design of new antibacterial agents. The crystal structures of Streptococcus pneumoniae GlmU in unbound form, in complex with acetyl-coenzyme A (AcCoA) and in complex with both AcCoA and the end product UDP-GlcNAc, have been determined and refined to 2.3, 2.5, and 1.75 Å, respectively. The S. pneumoniae GlmU molecule is organized in two separate domains connected via a long alpha -helical linker and associates as a trimer, with the 50-Å-long left-handed beta -helix (Lbeta H) C-terminal domains packed against each other in a parallel fashion and the C-terminal region extended far away from the Lbeta H core and exchanged with the beta -helix from a neighboring subunit in the trimer. AcCoA binding induces the formation of a long and narrow tunnel, enclosed between two adjacent Lbeta H domains and the interchanged C-terminal region of the third subunit, giving rise to an original active site architecture at the junction of three subunits.

* This work was funded in part by a Groupement d'Intérèt Public-Hoechst Marion Roussel grant and the Centre National de la Recherche Scientifique (UMR 6098, Marseille, France).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 1HM0, 1HM8, and 1HM9) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

§ Former post-doctoral fellow of Hoechst Marion Roussel. Holder of an EMBO fellowship.

Present address: ENSBANA, Département de Microbiologie, 1 Esplanade Erasme, 21000 Dijon, France. Former post-doctoral fellow of Hoechst Marion Roussel.

** 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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