PMID:9791115
| Citation |
Di Guilmi, AM, Mouz, N, Andrieu, JP, Hoskins, J, Jaskunas, SR, Gagnon, J, Dideberg, O and Vernet, T (1998) Identification, purification, and characterization of transpeptidase and glycosyltransferase domains of Streptococcus pneumoniae penicillin-binding protein 1a. J. Bacteriol. 180:5652-9 |
|---|---|
| Abstract |
Resistance to beta-lactam antibiotics in Streptococcus pneumoniae is due to alteration of penicillin-binding proteins (PBPs). S. pneumoniae PBP 1a belongs to the class A high-molecular-mass PBPs, which harbor transpeptidase (TP) and glycosyltransferase (GT) activities. The GT active site represents a new potential target for the generation of novel nonpenicillin antibiotics. The 683-amino-acid extracellular region of PBP 1a (PBP 1a*) was expressed in Escherichia coli as a GST fusion protein. The GST-PBP 1a* soluble protein was purified, and its domain organization was revealed by limited proteolysis. A protease-resistant fragment spanning Ser 264 to Arg 653 exhibited a reactivity profile against both beta-lactams and substrate analogues similar to that of the parent protein. This protein fragment represents the TP domain. The GT domain (Ser 37 to Lys 263) was expressed as a recombinant GST fusion protein. Protection by moenomycin of the GT domain against trypsin degradation was interpreted as an interaction between the GT domain and the moenomycin. |
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| Keywords |
Bacterial Proteins; Carrier Proteins; Endopeptidases/metabolism; Glutathione Transferase; Glycosyltransferases/chemistry; Glycosyltransferases/genetics; Glycosyltransferases/isolation & purification; Glycosyltransferases/metabolism; Hexosyltransferases/chemistry; Hexosyltransferases/genetics; Hexosyltransferases/isolation & purification; Hexosyltransferases/metabolism; Multienzyme Complexes/chemistry; Multienzyme Complexes/genetics; Multienzyme Complexes/isolation & purification; Multienzyme Complexes/metabolism; Muramoylpentapeptide Carboxypeptidase; Penicillin-Binding Proteins; Peptide Fragments; Peptide Mapping; Peptidyl Transferases/chemistry; Peptidyl Transferases/genetics; Peptidyl Transferases/isolation & purification; Peptidyl Transferases/metabolism; Recombinant Fusion Proteins/chemistry; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/isolation & purification; Recombinant Fusion Proteins/metabolism; Solubility; Streptococcus pneumoniae/enzymology; Trypsin/chemistry |
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