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A gene fusion that localises the penicillin-binding domain of penicillin-binding protein 3 of Escherichia coli
- Source :
- FEBS Letters. (1):179-184
- Publisher :
- Published by Elsevier B.V.
-
Abstract
- A gene fusion that links the COOH-terminal 349 amino acids of penicillin-binding protein 3 (60 kDa) of E.coli to the NH2-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.
- Subjects :
- DNA, Bacterial
Vesicle-associated membrane protein 8
Penicillin binding proteins
DNA, Recombinant
Biophysics
Carboxypeptidases
Penicillins
Peptidoglycan
Muramoylpentapeptide Carboxypeptidase
Biochemistry
Fusion gene
Bacterial Proteins
Structural Biology
Protein A/G
HSPA2
Genetics
polycyclic compounds
Escherichia coli
Penicillin-Binding Proteins
Transglycosylase-transpeptidase
Molecular Biology
biology
β-Lactam antibiotic
Escherichia coli Proteins
Penicillin-binding protein
Penicillin G
DNA Restriction Enzymes
Cell Biology
beta-Galactosidase
Fusion protein
Molecular biology
Peptide Fragments
Hexosyltransferases
Peptidyl Transferases
biology.protein
Penicillin binding
Peptidoglycan Glycosyltransferase
Protein G
Carrier Proteins
Gene fusion
Subjects
Details
- Language :
- English
- ISSN :
- 00145793
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....c57be6e1f3a732d2f701985ac4673b93
- Full Text :
- https://doi.org/10.1016/0014-5793(84)80936-9