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A gene fusion that localises the penicillin‐binding domain of penicillin‐binding protein 3 of Escherichia coli
Author(s) -
Hedge Philip J.,
Spratt Brian G.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80936-9
Subject(s) - penicillin binding proteins , benzylpenicillin , fusion protein , escherichia coli , penicillin , chemistry , biochemistry , binding domain , gene , amino acid , binding site , antibiotics , recombinant dna
A gene fusion that links the COOH‐terminal 349 amino acids of penicillin‐binding protein 3 (60 kDa) of E.coli to the NH 2 ‐terminus of β‐galactosidase has been constructed. The fusion protein (38.5 kDa) retains the ability to bind benzylpenicillin with high affinity, establishing that the penicillin‐binding domain (and presumably the penicillin‐sensitive transpeptidase activity) of this high molecular mass penicillin‐binding protein is located on a COOH‐terminal functional domain.