X-ray studies of enzymes that interact with penicillins.

Bacterial Proteins; Carrier Proteins/chemistry/metabolism; Crystallography, X-Ray; Hexosyltransferases; Models, Molecular; Muramoylpentapeptide Carboxypeptidase/chemistry/metabolism; Penicillin-Binding Proteins; Penicillins/chemistry/metabolism; Peptidyl Transferases; X-Ray Diffraction/methods; beta-Lactamases/chemistry/metabolism

Abstract :

[en] The technique of X-ray diffraction has been successfully applied to enzymes associated with peptidoglycan biosynthesis. The technique has taught us a great deal about the structures and catalytic mechanisms of penicillin-binding proteins and beta-lactamases. An insight into the structural basis for antibiotic resistance is given.

Disciplines :

Biochemistry, biophysics & molecular biology

Author, co-author :

Kelly, J. A.

Kuzin, A. P.

Charlier, Paulette ; Université de Liège - ULiège > Département des sciences de la vie > Cristallographie des macromolécules biologiques

Fonze, E.

Language :

English

Title :

X-ray studies of enzymes that interact with penicillins.

Publication date :

1998

Journal title :

Cellular and Molecular Life Sciences

ISSN :

1420-682X

eISSN :

1420-9071

Publisher :

Birkhäuser, Basel, Switzerland

Volume :

Issue :

Pages :

353-8

Peer reviewed :

Peer Reviewed verified by ORBi

Available on ORBi :

since 28 November 2010

Statistics

Number of views

222 (0 by ULiège)

Number of downloads

352 (0 by ULiège)

More statistics

Scopus citations^®

Scopus citations^®
without self-citations

OpenCitations

OpenAlex citations

Bibliography

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