K. Bush, G. A. Jacoby, and A. A. Medeiros, A functional classification scheme for beta-lactamases and its correlation with molecular structure, Antimicrobial Agents and Chemotherapy, vol.39, issue.6, pp.1211-1233, 1995.

J. R. Edwards, Errata, Journal of Antimicrobial Chemotherapy, vol.36, issue.5, pp.883-883, 1995.

J. L. Blumer, J. Infect. Dis. Suppl, vol.96, pp.38-44, 1995.

R. Labia, A. Morand, K. Tiwari, D. Sirot, and C. Chanal, J. Antimicrob. Chemother, vol.24, pp.219-223, 1989.

M. Galleni, G. Amicosante, and J. M. Frère, A survey of the kinetic parameters of class C ?-lactamases. Cephalosporins and other ?-lactam compounds, Biochemical Journal, vol.255, issue.1, pp.123-129, 1988.

P. Taibi and S. Mobashery, Mechanism of turnover of imipenem by the TEM .beta.-lactamase revisited, Journal of the American Chemical Society, vol.117, issue.29, pp.7600-7605, 1995.

Y. Yang, N. Bhachech, and K. Bush, Biochemical comparison of imipenem, meropenem and biapenem: permeability, binding to penicillin-binding proteins, and stability to hydrolysis by ?-lactamases, Journal of Antimicrobial Chemotherapy, vol.35, issue.1, pp.75-84, 1995.

D. M. Livermore, Carbapenemases, Journal of Antimicrobial Chemotherapy, vol.29, issue.6, pp.609-613, 1992.

A. Felici and G. Amicosante, Kinetic analysis of extension of substrate specificity with Xanthomonas maltophilia, Aeromonas hydrophila, and Bacillus cereus metallo-beta- lactamases, Antimicrobial Agents and Chemotherapy, vol.39, issue.1, pp.192-199, 1995.

A. Carfi, S. Pares, E. Duée, M. Galleni, C. Duez et al., The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold., The EMBO Journal, vol.14, issue.20, pp.4914-4921, 1995.

N. O. Concha, B. A. Rasmussen, K. Bush, and O. Herzberg, Crystal structure of the wide-spectrum binuclear zinc ?-lactamase from Bacteroides fragilis, Structure, vol.4, issue.7, pp.823-836, 1996.

P. Nordmann, S. Mariotte, T. Naas, R. Labia, and M. H. Nicolas, Biochemical properties of a carbapenem-hydrolyzing beta-lactamase from Enterobacter cloacae and cloning of the gene into Escherichia coli., Antimicrobial Agents and Chemotherapy, vol.37, issue.5, pp.939-946, 1993.

B. A. Rasmussen, K. Bush, D. Keeney, Y. Yang, R. Hare et al., Characterization of IMI-1 beta-lactamase, a class A carbapenem-hydrolyzing enzyme from Enterobacter cloacae., Antimicrobial Agents and Chemotherapy, vol.40, issue.9, pp.2080-2086, 1996.

T. Naas, L. Vandel, W. Sougakoff, D. M. Livermore, and P. Nordmann, Cloning and sequence analysis of the gene for a carbapenem-hydrolyzing class A beta-lactamase, Sme-1, from Serratia marcescens S6., Antimicrobial Agents and Chemotherapy, vol.38, issue.6, pp.1262-1270, 1994.

B. A. Rasmussen and K. Bush, Carbapenem-hydrolyzing beta-lactamases., Antimicrobial Agents and Chemotherapy, vol.41, issue.2, pp.223-232, 1997.

, Figure 13?figure supplement 1. Initial structures in systems (A) M1 (POPC/cholesterol/PI(4,5)P2 (65/29.5/5.5 composition on the cytosolic side interacting with FGF2); see text and Table 1) and (B) M2 (a single PI(4,5)P2 molecule allowed to interact with FGF2)., Superimposition of NMC-A (black) and of the acyl-enzyme complex TEM-1-6?-hydroxymethyl penicillanic acid

S. Mariotte-boyer, M. H. Nicolas-chanoine, and R. Labia, A kinetic study of NMC-A β-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycins, FEMS Microbiology Letters, vol.143, issue.1, pp.29-33, 1996.

X. Raquet, J. Lamotte-brasseur, F. Bouillenne, and J. Frère, A disulfide bridge near the active site of carbapenem-hydrolyzing class A ?-lactamases might explain their unusual substrate profile, Proteins: Structure, Function, and Genetics, vol.27, issue.1, pp.47-58, 1997.

W. Sougakoff, V. Jarlier, J. Delettré, N. Colloc'h, G. L'hermite et al., Purification, Crystallization, and Preliminary X-Ray Diffraction Analysis of the Carbapenem-Hydrolyzing Class A ?-Lactamase Sme-1 fromSerratia marcescens, Journal of Structural Biology, vol.116, issue.2, pp.313-316, 1996.

C. R. Cantor and P. R. Schimmel, Biophysical Chemistry, pp.374-385, 1980.

A. G. Leslie, Computational Aspects of Protein Crystal Data Analysis, Proceedings of the Daresbury Study Weekend, pp.39-50, 1987.

Z. Otwinowski, W. Wolf, P. R. Evans, and L. , Isomorphous Replacement and Anomalous Scattering, Proceedings of the CCP4 Study Weekend, pp.80-86, 1991.

. Collaborative-computational-project,-number-4, The CCP4 suite: programs for protein crystallography, Acta Crystallographica Section D Biological Crystallography, vol.50, issue.5, pp.760-763, 1994.

K. D. Cowtan, Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography, pp.34-38, 1994.

A. T. Brü-nger, Theoretical nuclear physics at Yale University, 1992.

T. A. Jones, J. Y. Zou, S. W. Cowan, and M. Kjeldgaard, Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallographica Section A Foundations of Crystallography, vol.47, issue.2, pp.110-119, 1991.

A. T. Brü-nger, Free R value: a novel statistical quantity for assessing the accuracy of crystal structures, Nature, vol.355, issue.6359, pp.472-475, 1992.

A. J. Wilson, The probability distribution of X-ray intensities, Acta Crystallographica, vol.2, issue.5, pp.318-321, 1949.

V. Luzzati, Traitement statistique des erreurs dans la determination des structures cristallines, Acta Crystallographica, vol.5, issue.6, pp.802-810, 1952.

O. Herzberg, Refined crystal structure of ?-lactamase from Staphylococcus aureus PC1 at 2.0 Å resolution, Journal of Molecular Biology, vol.217, issue.4, pp.701-719, 1991.

J. R. Knox and P. C. Moews, ?-Lactamase of Bacillus licheniformis 749/C, Journal of Molecular Biology, vol.220, issue.2, pp.435-455, 1991.

N. C. Strynadka, H. Adachi, S. E. Jensen, K. Johns, A. Sielecki et al., Molecular structure of the acyl-enzyme intermediate in ?-lactam hydrolysis at 1.7 Å resolution, Nature, vol.359, issue.6397, pp.700-705, 1992.

C. Jelsch, L. Mourey, J. Masson, and J. Samama, Crystal structure ofEscherichia coli TEM1 ?-lactamase at 1.8 Å resolution, Proteins: Structure, Function, and Genetics, vol.16, issue.4, pp.364-383, 1993.

J. R. Knox, P. C. Moews, and J. Frere, Molecular evolution of bacterial ?-lactam resistance, Chemistry & Biology, vol.3, issue.11, pp.937-947, 1996.

L. Maveyraud, I. Massova, C. Birck, K. Miyashita, J. Samama et al., Crystal Structure of 6?-(Hydroxymethyl)penicillanate Complexed to the TEM-1 ?-Lactamase fromEscherichia coli: Evidence on the Mechanism of Action of a Novel Inhibitor Designed by a Computer-Aided Process, Journal of the American Chemical Society, vol.118, issue.32, pp.7435-7440, 1996.

N. C. Strynadka, R. Martin, S. E. Jensen, M. Gold, and J. B. Jones, Structure-based design of a potent transition state analogue for TEM-1 ?-lactamase, Nature Structural & Molecular Biology, vol.3, issue.8, pp.688-695, 1996.

L. E. Zawadzke, C. C. Chen, S. Banerjee, Z. Li, S. Wäsch et al., Elimination of the Hydrolytic Water Molecule in a Class A ?-Lactamase Mutant: Crystal Structure and Kinetics?,?, Biochemistry, vol.35, issue.51, pp.16475-16482, 1996.

L. Maveyraud, R. F. Pratt, and J. Samama, Crystal Structure of an Acylation Transition-State Analog of the TEM-1 ?-Lactamase. Mechanistic Implications for Class A ?-Lactamases?, Biochemistry, vol.37, issue.8, pp.2622-2628, 1998.

L. E. Zawadzke, T. J. Smith, and O. Herzberg, An engineered Staphylococcus aureus PCI ß-lactamase that hydrolyses third-generation cephalosporins, "Protein Engineering, Design and Selection", vol.8, issue.12, pp.1275-1285, 1995.

S. Banerjee, U. Pieper, G. Kapadia, L. K. Pannell, and O. Herzberg, Role of the ?-Loop in the Activity, Substrate Specificity, and Structure of Class A ?-Lactamase?,?, Biochemistry, vol.37, issue.10, pp.3286-3296, 1998.

J. R. Knox, Extended-spectrum and inhibitor-resistant TEM-type beta-lactamases: mutations, specificity, and three-dimensional structure, Antimicrobial Agents and Chemotherapy, vol.39, issue.12, pp.2593-2601, 1995.

A. Hutlesky, J. R. Knox, and R. C. Levesque, J. Biol. Chem, vol.268, pp.3690-3697, 1993.

X. Raquet, J. Lamotte-brasseur, E. Fonzé, S. Goussard, P. Courvalin et al., TEM ?-Lactamase Mutants Hydrolysing Third-generation Cephalosporins, Journal of Molecular Biology, vol.244, issue.5, pp.625-639, 1994.

J. Osuna, H. Viadiu, A. L. Fink, and X. Soberon, J. Biol. Chem, vol.270, pp.775-780, 1995.

K. Miyashita, I. Massova, and S. Mobashery, Quantification of the extent of attenuation of the rate of turnover chemistry of the TEM-1 ?-lactamase by the ?-1R-hydroxyethyl group in substrates, Bioorganic & Medicinal Chemistry Letters, vol.6, issue.3, pp.319-322, 1996.