|
pubmed:abstractText |
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.
|
