PMID:9158725
| Citation |
Fusetti, F and Dijkstra, BW (1996) Purification and light-scattering analysis of penicillin-binding protein 4 from Escherichia coli. Microb. Drug Resist. 2:73-6 |
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| Abstract |
Penicillin binding protein 4 (PBP4) from Escherichia coli is a protein involved in the recycling and maturation of the bacterial cell wall and it is inhibited by beta-lactam antibiotics. PBP4 exhibits D-Ala-D-Ala-endopeptidase as well as D-Ala-D-Ala-carboxypeptidase activity. To provide a structural template for the design of new, more specific antibiotics we started X-ray crystallographic studies of penicillin binding protein 4 from Escherichia coli. PBP4 has been overexpressed in Escherichia coli as a His-tagged protein. A large-sclae purification scheme, yielding a very pure material, has been set up and crystallization experiments have been started. Dynamic light scattering experiments suggested that PBP4 exhibits aggregation behavior with a number of different precipitating agents and additives. Only by addition of EDTA, PEG 4000, and ammonium sulfate is the molecular mass about 110 kDa. |
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| Keywords |
Bacterial Proteins; Carrier Proteins/analysis; Carrier Proteins/genetics; Carrier Proteins/isolation & purification; Chelating Agents; Crystallography, X-Ray; Electrophoresis, Polyacrylamide Gel; Escherichia coli/chemistry; Escherichia coli/genetics; Escherichia coli Proteins; Hexosyltransferases; Light; Molecular Weight; Muramoylpentapeptide Carboxypeptidase/analysis; Muramoylpentapeptide Carboxypeptidase/genetics; Muramoylpentapeptide Carboxypeptidase/isolation & purification; Penicillin-Binding Proteins; Penicillins/metabolism; Peptidyl Transferases; Plasmids/genetics; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Scattering, Radiation; Serine-Type D-Ala-D-Ala Carboxypeptidase |
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