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Originally published In Press as doi:10.1074/jbc.M003802200 on May 23, 2000

J. Biol. Chem., Vol. 275, Issue 36, 28075-28082, September 8, 2000
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The High Resolution Crystal Structure for Class A beta -Lactamase PER-1 Reveals the Bases for Its Increase in Breadth of Activity*

Samuel TranierDagger , Anne-Typhaine Bouthors§, Laurent MaveyraudDagger , Valérie GuilletDagger , Wladimir Sougakoff§, and Jean-Pierre SamamaDagger

From the Dagger  Groupe de Cristallographie Biologique, Institut de Pharmacologie et de Biologie Structurale du CNRS, 205 route de Narbonne, F-31077 Toulouse cedex, France and the § Laboratoire de Recherche Moléculaire sur les Antibiotiques, Faculté de Médecine Pitié-Salpêtrière, Université Pierre et Marie Curie, F-75634 Paris cedex, France

The treatment of infectious diseases by beta -lactam antibiotics is continuously challenged by the emergence and dissemination of new beta -lactamases. In most cases, the cephalosporinase activity of class A enzymes results from a few mutations in the TEM and SHV penicillinases. The PER-1 beta -lactamase was characterized as a class A enzyme displaying a cephalosporinase activity. This activity was, however, insensitive to the mutations of residues known to be critical for providing extended substrate profiles to TEM and SHV. The x-ray structure of the protein, solved at 1.9-Å resolution, reveals that two of the most conserved features in class A beta -lactamases are not present in this enzyme: the fold of the Omega -loop and the cis conformation of the peptide bond between residues 166 and 167. The new fold of the Omega -loop and the insertion of four residues at the edge of strand S3 generate a broad cavity that may easily accommodate the bulky substituents of cephalosporin substrates. The trans conformation of the 166-167 bond is related to the presence of an aspartic acid at position 136. Selection of class A enzymes based on the occurrence of both Asp136 and Asn179 identifies a subgroup of enzymes with high sequence homology.

* This work was supported by Institut National de la Santé et de la Recherche Médicale Grants CRI 950601 and E0004, by the Ministère de la Recherche (PRFMMIP: Réseau de Recherche sur les beta -Lactamases), and by the Centre National de la Recherche Scientifique.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 1e25) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

To whom correspondence should be addressed. Tel.: 33 5 61 17 54 44; Fax: 33 5 61 17 54 48; E-mail: samama@ipbs.fr.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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