Reference : 2.8-Å Structure of penicillin-sensitive D-alanyl carboxypeptidase-transpeptidase from...
Scientific journals : Article
Life sciences : Microbiology
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/83013
2.8-Å Structure of penicillin-sensitive D-alanyl carboxypeptidase-transpeptidase from Streptomyces R61 and complexes with β-lactams
English
Kelly, Judith A [University of Connecticut - UCONN > School of Pharmacy, and Institute of Materials Science > Biological Sciences Group > > >]
Knox, James R [University of Connecticut - UCONN > School of Pharmacy, and Institute of Materials Science > Biological Sciences Group > > >]
Moews, Paul C [University of Connecticut - UCONN > School of Pharmacy, and Institute of Materials Science > Biological Sciences Grou > > >]
Hite, Gilbert J [University of Connecticut - UCONN > School of Pharmacy, and Institute of Materials Science > Biological Sciences Group > > >]
Bartolone, John B [University of Connecticut - UCONN > School of Pharmacy, and Institute of Materials Science > Biological Sciences Group > > >]
Zhao, Haiching [University of Connecticut - UCONN > School of Pharmacy, and Institute of Materials Science > Biological Sciences Group > > >]
Joris, Bernard mailto [Université de Liège - ULiège > Faculté de Médecine > Service de Microbiologie > >]
Frère, Jean-Marie mailto [Université de Liège - ULiège > Faculté de Médecine > Service de Microbiologie > >]
Ghuysen, Jean-Marie [Université de Liège - ULiège > Faculté de Médecine > Service de Microbiologie > > >]
25-May-1985
Journal of Biological Chemistry
American Society for Biochemistry and Molecular Biology
260
10
6449-6458
Yes (verified by ORBi)
International
0021-9258
1083-351X
Baltimore
MD
[en] anti-bacterial agents ; binding sites ; carboxypeptidases/metabolism ; models, molecular ; muramoylpentapeptide carboxypeptidase/metabolism ; protein conformation ; streptomyces/*enzymology ; x-ray diffraction ; beta-Lactams
[en] The crystallographic structure of the penicillin-sensitive D-alanyl carboxypeptidase-transpeptidase from Streptomyces R61 has been solved to 2.8-A resolution. The 38,000-dalton serine peptidase has two regions of secondary structure, an alpha/beta cluster, and a region which contains five helical segments. The beta sheet is composed of five beta strands. The tertiary structure has no homology with the classic serine proteases or with the zinc carboxypeptidases. The binding at a common site of three types of beta-lactam (a penicillin, a cephalosporin, a monocyclic beta-lactam) and a desazacyclobutanone has been observed in Fourier difference maps. The binding site sequence is Val-Gly-Ser-Val-Thr-Lys. The beta-lactam ring lies near the enzyme's catalytic serine at position 37, and the C3 substituent of a cephalosporin falls near lysine 40.
Researchers ; Professionals
http://hdl.handle.net/2268/83013

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