β-Lactamase of Bacillus licheniformis 749/C

Ambler, 1991, A standard numbering scheme for class A β-lactamases, Biochem. J., 10.1042/bj2760269 Baker, 1988, Structure of Azurin from Alcaligenes denitrificans. Refinement at 1.8 Å resolution and comparison of the two crystallographically independent molecules, J. Mol. Biol., 203, 1071, 10.1016/0022-2836(88)90129-5 Baker, 1984, Hydrogen bonding in globular proteins, Progr. Biophys. Molec. Biol., 44, 97, 10.1016/0079-6107(84)90007-5 Brünger, 1988 Burley, 1985, Aromatic-aromatic interaction: A mechanism of protein structure stabilization, Science, 229, 23, 10.1126/science.3892686 Cartwright, 1989, Trapping the acyl-enzyme intermediate in β-lactamase I catalysis, Biochem. J., 263, 905, 10.1042/bj2630905 Chou, 1977, β-Turns in proteins, J. Mol. Biol., 115, 135, 10.1016/0022-2836(77)90094-8 Chou, 1985, Interactions between an α-helix and a β-sheet, J. Mol. Biol., 186, 591, 10.1016/0022-2836(85)90133-0 Christensen, 1990, β-Lactamases as fully efficient enzymes, Biochem. J., 266, 853 Dideberg, 1987, The crystal structure of the βlaetamase of Streptomyces albus G at 0.3 nm resolution, Biochem. J., 245, 911, 10.1042/bj2450911 Ellerby, 1990, The role of lysine-234 in β-lactamase catalysis probed by site-directed mutagenesis, Biochemistry, 29, 5797, 10.1021/bi00476a022 Finzel, 1987, Structure of ferricytochrome ć of Rhodospirillum molischianum at 1.67 Å resolution, J. Mol. Biol., 186, 627, 10.1016/0022-2836(85)90135-4 Healey, 1989, Substrate specificities in class A β-lactamases. Preference for penams vs cephems. The role of residue 237, Protein Struct. Fund. Genet., 6, 275, 10.1002/prot.340060310 Herzberg, 1987, Bacterial resistance to β-lactam antibiotics: Crystal structure of β-lactamase from Staphylococcus aureus PC1 at 2.5 Å resolution, Science, 236, 694, 10.1126/science.3107125 Jacob, 1990, Role of the conserved amino acids of the “SDN” loop in a class A α-lactamase studied by site-directed mutagenesis, Biochem. J., 271, 399, 10.1042/bj2710399 Jones, 1985, Interactive computer graphics: FRODO, Methods Enzymol., 115, 157, 10.1016/0076-6879(85)15014-7 Juteau, 1990, Site saturation mutagenesis of ROB-1 β-lactamase at residue serine 130 Kabsch, 1983, Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features, Biopolymers, 22, 2577, 10.1002/bip.360221211 Kelly, 1986, On the origin of bacterial resistance to penicillin: Comparison of a β-lactamase and a penicillin target, Science, 231, 1429, 10.1126/science.3082007 Kelly, 1989, Crystallographic mapping of β-lactams bound to a DD-peptidase, J. Mol. Biol., 209, 281, 10.1016/0022-2836(89)90277-5 Knox, 1989, Crystallographic comparison of penicillin-recognizing enzymes, 46 Konnert, 1980, A restrained-parameter thermal-factor refinement procedure, Acta Crystallogr. sect. A, 36, 344, 10.1107/S0567739480000794 Leszczynski, 1986, Loops in globular proteins: A novel category of secondary structure, Science, 234, 849, 10.1126/science.3775366 Luzzati, 1952, Traitement statistique des erreurs dans la détermination des structures cristallines, Acta Crystallogr., 5, 802, 10.1107/S0365110X52002161 Matagne, 1990, The diversity of the catalytic properties of class A β-lactamases, Biochem. J., 265, 131, 10.1042/bj2650131 Moews, 1990, β-Lactamase of Bacillus licheniformis 749/C at 2 Å resolution, Proteins Struct. Funct. Genet., 7, 156, 10.1002/prot.340070205 Murphy, 1988, Evidence for an oxyanion hole in serine α-lactamases and DD-peptidases, Biochem. J., 256, 669, 10.1042/bj2560669 Oefner, 1990, Refined crystal structure of β-lactamase of Citrobacter freundii indicates a mechanism for β-lactam hydrolysis, Nature (London), 343, 284, 10.1038/343284a0 Pratt, 1988, Accumulation of an acyl-enzyme intermediate during turnover of penicillin by the class A β-lactamase of Saureus PC1, Biochem. J., 254, 919, 10.1042/bj2540919 Presta, 1988, Helix signals in proteins, Science, 240, 1631, 10.1126/science.2837824 Read, 1986, Improved Fourier coefficients for maps using phases from partial structures with errors, Acta Crystallogr. sect. A., 42, 140, 10.1107/S0108767386099622 Richardson, 1981, The anatomy and taxonomy of protein folding, Advan. Protein Chem., 34, 167, 10.1016/S0065-3233(08)60520-3 Richardson, 1988, Amino acid preferences for specific locations at the ends of α-helices, Science, 240, 1648, 10.1126/science.3381086 Richardson, 1989, Principles and patterns of protein conformation, 1 Samraoui, 1986, Tertiary structural similarity between a class A β-lactamase and a penicillin-sensitive d-alanyl carboxypeptidasetranspeptidase, Nature (London), 320, 378, 10.1038/320378a0 Sheriff, 1987, The structure of myohemerythrin in the azidomet state at 1.71.3 Å resolution, J. Mol. Biol., 197, 273, 10.1016/0022-2836(87)90124-0 Sobottka, 1984, A MWPC X-ray diffractometer facility for protein crystallography, Nucl. Instrum. Methods, 220, 575, 10.1016/0167-5087(84)90325-9 Stewart, 1972, The X-ray system of crystallographic programs Sutton, 1987, An X-ray crystallographies study of β-lactamase II from Bacillus cereus at 0.35 nm resolution, Biochem J., 248, 181, 10.1042/bj2480181 Wlodawer, 1987, Comparison of two highly refined structures of bovine pancreatic trypsin inhibitor, J. Mol. Biol., 193, 145, 10.1016/0022-2836(87)90633-4