Article (Scientific journals)
X-ray studies of enzymes that interact with penicillins.
Kelly, J. A.; Kuzin, A. P.; Charlier, Paulette et al.
1998In Cellular and Molecular Life Sciences, 54 (4), p. 353-8
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Keywords :
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 :
54
Issue :
4
Pages :
353-8
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 28 November 2010

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