Article (Scientific journals)
Penicillin target enzyme and the antibiotic binding site
Kelly, Judith A.; Moews, Paul C.; Knox, James R. et al.
1982In Science, 218 (4571), p. 479-481
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Keywords :
binding sites; carboxypeptidases; cephalosporins; crystallography; models, molecular; muramoylpentapeptide carboxypeptidase; penicillins; protein conformation; x-ray diffraction
Abstract :
[en] The three-dimensional structure of a penicillin-sensitive D-alanyl-carboxypeptidase-transpeptidase has been determined by x-ray crystallography to a resolution of 2.8 angstroms. The site of binding of the beta-lactam antibiotics penicillin and cephalosporin has been located. These findings constitute direct observation of the interaction of beta-lactams with a transpeptidase enzyme and establish the feasibility of defining the molecular stereochemistry of this interaction for purposes of drug design.
Disciplines :
Biochemistry, biophysics & molecular biology
Microbiology
Author, co-author :
Kelly, Judith A.;  University of Connecticut - UCONN > Biologicale Sciences Group - Institut of Material Science
Moews, Paul C.;  University of Connecticut - UCONN > Biologicale Sciences Group - Institut of Material Science
Knox, James R.;  University of Connecticut - UCONN > Biologicale Sciences Group - Institut of Material Science
Frère, Jean-Marie ;  Université de Liège - ULiège > Faculté de Médecine > Service de Microbiologie
Ghuysen, Jean-Marie ;  Université de Liège - ULiège > Faculté de Médecine > Service de Microbiologie
Language :
English
Title :
Penicillin target enzyme and the antibiotic binding site
Publication date :
29 October 1982
Journal title :
Science
ISSN :
0036-8075
eISSN :
1095-9203
Publisher :
American Association for the Advancement of Science, Washington, United States - District of Columbia
Volume :
218
Issue :
4571
Pages :
479-481
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 17 June 2011

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