X-ray studies of enzymes that interact with penicillins

Cellular and Molecular Life Sciences

Volumn 54, Issue 4, 1998, Pages 353-358

  Kelly, J A ^a   Kuzin, A P ^a   Charlier, P ^b   Fonze E ^b  

^a UNIVERSITY OF CONNECTICUT   (United States)

^b UNIVERSITY OF LIÈGE   (Belgium)

Author keywords

lactamases; Active site serine; Penicillin binding proteins; Peptidases; X ray diffraction

Indexed keywords

BETA LACTAMASE; PENICILLIN BINDING PROTEIN; PENICILLIN DERIVATIVE; PEPTIDOGLYCAN;

ANTIBIOTIC RESISTANCE; BIOSYNTHESIS; CONFERENCE PAPER; NONHUMAN; STRUCTURE ACTIVITY RELATION; X RAY DIFFRACTION;

BACTERIAL PROTEINS; BETA-LACTAMASES; CARRIER PROTEINS; CRYSTALLOGRAPHY, X-RAY; HEXOSYLTRANSFERASES; MODELS, MOLECULAR; MURAMOYLPENTAPEPTIDE CARBOXYPEPTIDASE; PENICILLIN-BINDING PROTEINS; PENICILLINS; PEPTIDYL TRANSFERASES; X-RAY DIFFRACTION;

EID: 0031898283     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050163     Document Type: Conference Paper

References (14)

1. Ghuysen J.-M. (1991) Serine β-lactamases and penicillin-binding proteins. Ann. Rev. Microb. 45: 37-65
2. Despreaux C. W. and Manning R. F. (1993) The dacA gene of Bacillus stearothermophilus coding for D-alanine carboxypeptidase: cloning, structure and expression in E. coli and Pichia pastoris. Gene 131: 35-41
3. Nguyen-Distèche M., Leyh-Bouille M., Pirlot S., Frère J.-M. and Ghuysen J.-M. (1986) Streptomyces K15 DD-peptidase-catalysed reactions with ester and amide carbonyl donors. Biochem. J. 235: 167-176
4. Kelly J. A. and Kuzin A. P. (1995) The refined crystallographic structure of a DD-peptidase penicillin-target enzyme at 1.6 Å resolution. J. Mol. Biol. 254: 223-236
5. Fonzé E., Charlier P., Tóth Y., Vermeire M., Raquet X. and Frère J.-M. (1995) THM1 β-lactamase structure solved by molecular replacement and refined structure of the S235A mutant. Acta Cryst. D51: 682-694
6. Strynadka N. C. J., Adachi H., Jensen S. E., Johns H., Sielecki A., Betzel C. et al. (1992) Molecular structure of the acyl-enzyme intermediate in β-lactam hydrolysis at enzyme at 1.7 Å resolution. Nature (Lond.) 359: 700-705
7. Chen C. C. H. and Herzberg O. (1992) Inhibition of β-lactamases by clavulanate. Trapped intermediates in cryocristallographic studies. J. Mol. Biol. 224: 1103-1113
8. Chen C. C. H., Rahil J., Pratt R. F. and Herzberg O. (1993) Structure of a phosphonate-inhibited β-lactamase: an analog of the tetrahedral transition state intermediate of β-lactam hydrolysis. J. Mol. Biol. 234: 165-178
9. Maveyraud L., Massova I., Birck C., Miyashita K., Samama J.-P. and Mobashery S. (1996) Crystal structure of a 6α-(hydroxymethy)penicillanate complexed to the TEM1 β-lactamase from E. coli: evidence on the mechanism of action of a nov1 inhibitor designed by a computer-aided process. J. Am. Chem. Soc. 118: 7435-7440
10. Strynadka N. C. J., Martin R., Jensen S. H. Gold M. and Jones J. B. (1996) Structure-based design of a potent transition state analogue for the TEM-1 β-lactamase. Nature Struct. Biol. 3: 688-695
11. Oefner C., D'Arcy A., Daly J. J., Gubernator K., Charnas R. L., Heinze I. et al. (1990) Refined crystal structure of β-lactamase from Citrobacter freundii indicates a mechanism for β-lactam hydrolysis. Nature 343: 284-288
12. Lobkovsky E., Billings E. M., Moews P. C., Rahil J., Pratt R. F. and Knox J. R. (1994) Crystallographic structure of a phosphonate derivative of the Enterobacter cloacae P99 cephalosporinase: mechanistic interpretation of a β-lactamase transition state analog. Biochemistry 33: 6762-6772
13. Kuzin A. P., Liu H., Kelly J. A. and Knox J. R. (1995) Binding of cephalothin and cefotaxime to D-Ala-D-Ala peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum β-lactamases. Biochemistry 34: 9532-9540
14. Coffey T. J., Daniels M., McDougal L. K., Dowson C. G., Tenover F. C. and Spratt B. G. (1995) Genetic analysis of clinical isolates of Streptococcus pneumoniae with high-level resistance to expanded-spectrum cephalosporins. Antimicrob. Agents Chemother. 39: 1306-1313