Site-directed mutagenesis of penicillin-binding protein 3 of Escherichia coli: role of Val-545.
Val545 of the Escherichia coli penicillin-binding protein 3 is essential to the acyl transfer mechanism through which the active-site serine 307 is acylated by benzylpenicillin and cephalexin and to the mechanism through which the protein allows rapidly growing cells to divide.
Ayala
J
J
Centro de Biologia Molecular Severo Ochoa, Consejo Superior de Investigaciones Cientificas, Universidad Autonoma, Madrid, Spain.
Goffin
C
C
Nguyen-Distèche
M
M
Ghuysen
J M
JM
D001426:Bacterial Proteins; D001483:Base Sequence; D002352:Carrier Proteins / Q000235:genetics*; D018076:DNA, Complementary; D004926:Escherichia coli / Q000737:chemistry* / Q000235:genetics / Q000254:growth & development; D029968:Escherichia coli Proteins; D006602:Hexosyltransferases; D008969:Molecular Sequence Data; D002267:Muramoylpentapeptide Carboxypeptidase / Q000235:genetics*; D016297:Mutagenesis, Site-Directed; D046915:Penicillin-Binding Proteins; D046928:Peptidoglycan Glycosyltransferase; D010458:Peptidyl Transferases; D014633:Valine / Q000235:genetics
D001426:Bacterial Proteins; D002352:Carrier Proteins; D018076:DNA, Complementary; D029968:Escherichia coli Proteins; C478704:FtsI protein, E coli; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D046928:Peptidoglycan Glycosyltransferase; D002267:Muramoylpentapeptide Carboxypeptidase; D014633:Valine