Abola,E.E., Bernstein,F.C., Bryant,S.H., Koetzle,T.F. and Weng,J. (1987) Protein data base. In Allen,F.H., Bergerhoff,G. and Sievers,R. (eds), Crystallographic Databases - Information Content, Software Systems, Scientific Applications. Data Commission of the International Union of Crystallography, Bonn, Germany, pp. 107-132.
Ambler,R.P., Daniel,M., Fleming,J., Hermoso,J.M., Pang,C. and Waley,S.G. (1985) The amino acid sequence of the zinc-requiring β-lactamase II from the bacterium Bacillus cereus 569. FEBS Lett., 189, 207-211.
Baldwin,G.S., Galdes,A., Hill,H.A.O., Smith,B.E., Waley,S.G. and Abraham,E.P. (1978) Histidine residues as zinc ligands in β-lactamase II. Biochem. J., 175, 441-447.
Baldwin,G.S., Waley,S.G. and Abraham,E.P. (1979) Identification of histidine residues that act as zinc ligands in β-lactamase II by differential tritium exchange. Biochem. J., 179, 459-463.
Bicknell,R., Emanuel,E., Gagnon,J. and Waley,S.G. (1985) The production and molecular properties of the zinc β-lactamase of Pseudomonas maltophilia II D 1275. Biochem. J., 229, 791-797.
Bicknell,R., Shaffer,A., Waley,S.G. and Auld,D.S. (1986) Changes in the coordination geometry of the active-site metal during catalysis of benzylpenicillin hydrolysis by Bacillus cereus β-lactamase II. Biochemistry, 25, 7208-7215.
Brünger,A.T. (1992) A System for X-ray Crystallography and NMR: XPLOR. Version 3.0, Yale University Press, New Haven, CT.
Carson,M.C. (1991) RIBBONS 2.0. J. Appl. Cryst., 24, 958-961.
Clackson,T., Güssow,D. and Jones,P.T. (1991) In McPherson,M.J., Anirke,R and Taylor,G.R. (eds), PCR: A Practical Approach. IRL Press, Oxford, UK, pp. 202-203.
Clark,S.D. (1993) Site directed mutagenesis of bacterial metallo-β-lactamase. PhD Thesis, Texas Technical University, TX.
Crompton,I.E. and Waley,S.G. (1986) The determination of specificity constants in enzyme-catalysed reactions. Biochem. J., 239, 221-224.
Davies,R.B. and Abraham,E.P. (1974) Metal cofactor requirement of β-lactamase II. Biochem. J., 143, 129-135.
Dideberg,O., Charlier,P., Dive,G., Joris,B., Frère,J.M. and Ghuysen,J.M. (1982) Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 Å resolution. Nature, 299, 469-470.
Felici,A., Amicosante,G., Oratore,A., Strom,R., Ledent,R, Joris,B., Fanuel,L. and Frère,J.M. (1993) An overview of the kinetic parameters of class B β-lactamases. Biochem. J., 291, 151-155.
Gaboriaud,C., Bissery,V., Bencherit,T. and Mornon,J.P. (1987) Hydrophobic cluster analysis: an efficient new way to compare and analyse amino acid sequences. FEBS Lett., 224, 149-155.
Galdes,A., Hill,H.A.O., Baldwin,G.S., Waley,S.G. and Abraham,E.P. (1980) The 1H nuclear-magnetic-resonance spectroscopy of Cobalt(II)-β-lactamase II. Biochem. J., 187, 789-795.
Hooper,N.M. (1994) Families of zinc metalloproteases. FEBS Lett., 354, 1-6.
Hussain,M., Carlino,A., Madonna,M.J. and Lampen,J.O. (1985) Cloning and sequencing of the metallothioprotein β-lactamase II gene of Bacillus cereus 569/H in Escherichia coli. J. Bacteriol., 164, 223-229.
Jones,T.A., Zou,J.Y., Cowan,S.W. and Kjeldgaard,M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr., A47, 110-119.
Kabsch,W. (1988) Evaluation of single X-ray diffraction data from a position sensitive detector. J. Appl. Cryst., 21, 916-924.
Kabsch,W. (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmery and cell constants. J. Appl. Cryst., 26, 795-800.
Kato,C., Kudo,T., Watanabe,K. and Horikoshi,K. (1985) Nucleotide sequence of the β-lactamase gene of alkalophilic Bacillus sp. strain 170. J. Gen. Microbiol., 131, 3317-3324.
Kraulis,P.J. (1991) MOLSCRIPT. a program to produce both detailed and schematic plots of protein. J. Appl. Cryst. 24, 946-950.
Lim,H.M., Iyer,R.K. and Pene,J.J. (1991) Site-directed mutagenesis of dicarboxylic acids near the active site of Bacillus cereus 5/B/6 β-lactamase II. Biochem. J., 276, 401-404.
Lipman,D.J. and Pearson,W.R. (1985) Rapid and sensitive protein similarity searches. Science, 227, 1435-1441.
Lipscomb,W.N. (1983) Structure and catalysis of enzymes. Annu. Rev. Biochem., 52, 17-34.
Löwe,J., Stock,D., Jap,B., Zwickl,P., Baumeister,W. and Huber,R. (1995) Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution. Science, 268, 533-539.
Maniatis,T., Fritsh,E.F. and Sambrook,J. (1982) Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
Massidu,O., Rossolini,G.M. and Satta,G. (1991) The Aeromonas hydrophila A gene: molecular heterogeneity among class B metallo-β-lactamases. J. Bacteriol., 173, 4611-4617.
Matthews,B.W. (1988) Structural basis of the action of thermolysin and related zinc peptidases. Ace. Chem. Res., 21, 333-340.
Messerschmidt,A. and Pflugrath,J.W. (1987) Crystal orientation and X-ray pattern prediction routines for area-detector diffractometer systems in macromolecular crystallography. J. Appl. Cryst., 20, 306-315.
Mol,C.D., Kuo,C.-F., Thayer,M.M., Cunningham,R.P. and Tainer,J.A. (1995) Structure and function of the multifunctional DNA-repair enzyme exonuclease III. Nature, 374, 381-386.
Oefner,C. and Suck,D. (1986) Crystallographic refinement and structure of DNase I at 2 Å resolution. J. Mol. Biol., 192, 605-632.
Osano,E., Arakawa,Y., Wacharotayankun,R., Ohta,M., Horii,T., Ito,H., Yoshimura,F. and Kato,N. (1994) Molecular characterization of an enterobacterial metallo-β-lactamase found in a clinical isolate of Serratia marcescens that shows imipenem resistance. Antimicrob. Agents Chemother., 38, 71-78.
Payne,D.J. (1993) Metallo-β-lactamase: a new therapeutic challenge. J. Med. Microbiol., 39, 93-99.
Ramachandran,G.N., Ramakrishnan,C. and Sasisekharan,V. (1963) Stereochemistry of polypeptide chain configurations. J. Mol. Biol., 7, 95-99.
Rasmussen,B.A., Gluzman,Y. and Tally,F.P. (1990) Cloning and sequencing of the class B β-lactamase gene (ccrA) from Bacteroides fragilis TAL3636. Antimicrob. Agents Chemother., 34, 1590-1592.
Read,R.J. (1986) Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr., A42, 140-149.
Saino,Y., Kobayashi,F., Inoue,M. and Mitsuhashi,S. (1982) Purification and properties of inducible penicillin β-lactamase isolated from Pseudomonas maltophilia. Antimicrob. Agents Chemother., 22, 564-570.
Smith,J.L., Zaluzec,E.J., Wery,J.-P., Niu,L., Switzer,R.L., Zalkin,H. and Satow,Y. (1994) Structure of the allosteric regulatory enzyme of purine biosynthesis. Science, 264, 1427-1433.
Stöcker,W., Gomis-Rüth,F.-X., Bode,W. and Zwilling,R. (1993) Implications of the three-dimensional structure of astacin for the structure and function of the astacin family of zinc-endopeptidases. Eur. J. Biochem., 214, 215-231.
Stöcker,W., Grams,F., Baumann,U., Reinemer,P., Gomis-Rüth,F.-X., McKay,D.B. and Bode,W. (1995) The metzincins - Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases. Protein Sci., 4, 823-840.
Suck,D., Oefner,C. and Kabsch,W. (1984) Three-dimensional structure of bovine pancreatic DNase 1 at 2.5 Å resolution. EMBO J., 3, 2423-2430.
Sutton,B.J., Artymiuk,P.J., Cordero-Borboa,A.E., Little,C., Phillips,D.C. and Waley,S.G. (1987) An X-ray-crystallographic study of β-lactamase II from Bacillus cereus at 0.35 nm resolution. Biochem. J., 248, 181-188.
Thompson,J.S. and Malamy,M.H. (1990) Sequencing the gene of imipenem-cefoxitin-hydrolyzing enzyme (CfiA) from Bacteroides fragilis TAL2480 reveals strong similarity between CfiA and Bacillus cereus β-lactamase II. J. Bacteriol., 172, 2584-2593.
Waley,S.J. (1992) β-lactamase: mechanism of action. In Page,M. (ed.), The Chemistry of β-Lactams. Blackie Academic and Professional, Chapman and Hall, London, UK, pp. 198-228.
Walsh,T.R., Hall,L., Assinder,S.J., Nichols,W.W., Cartwright,S.J., MacGowan,A.P. and Bennett,P.M. (1994) Sequence analysis of the L1 metallo-β-lactamase from Xanthomonas maltophilia. Biochim. Biophys. Acta, 1218, 199-201.
Yang,Y, Wu,P. and Livermore,D.M. (1990) Biochemical characterization of a β-lactamase that hydrolyses penems and carbapenems from two Serratia marcescens isolates. Antimicrob. Agents Chemother., 34, 755-758.
