Primary and predicted secondary structures of the Actinomadura R39 extracellular dd -peptidase, a penicillin-binding protein (PBP) related to the Escherichia coli PBP4
| Autor: | B. Granier, Jean-Marie Frère, Colette Duez, J. Van Beeumen, Jean Dusart, Sophie Lepage, J M Ghuysen, Otto Dideberg, Serge Englebert |
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| Rok vydání: | 1992 |
| Předmět: |
Penicillin binding proteins
Chemical Phenomena Molecular Sequence Data Restriction Mapping Gene Expression Muramoylpentapeptide Carboxypeptidase medicine.disease_cause Biochemistry Streptomyces beta-Lactamases Bacterial Proteins Sequence Homology Nucleic Acid Actinomycetales Escherichia coli medicine Penicillin-Binding Proteins Actinomadura Amino Acid Sequence Cloning Molecular Molecular Biology Peptide sequence Protein secondary structure Streptomyces albus Base Sequence biology Chemistry Physical Protein primary structure Correction DNA Cell Biology biology.organism_classification Molecular Weight Hexosyltransferases Peptidyl Transferases Carrier Proteins Extracellular Space Research Article |
| Zdroj: | Biochemical Journal. 282:781-788 |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bj2820781 |
| Popis: | As derived from gene cloning and sequencing, the 489-amino-acid DD-peptidase/penicillin-binding protein (PBP) produced by Actinomadura R39 has a primary structure very similar to that of the Escherichia coli PBP4 [Mottl, Terpstra & Keck (1991) FEMS Microbiol. Lett. 78, 213-220]. Hydrophobic-cluster analysis of the two proteins shows that, providing that a large 174-amino-acid stretch is excluded from the analysis, the bulk of the two polypeptide chains possesses homologues of the active-site motifs and secondary structures found in the class A beta-lactamase of Streptomyces albus G of known three-dimensional structure. The 174-amino-acid insert occurs at equivalent places in the two PBPs, between helices alpha 2 and alpha 3, away from the active site. Such an insert is unique among the penicilloyl serine transferases. It is proposed that the Actinomadura R39 PBP and E. coli PBP4 form a special class, class C, of low-Mr PBPs/DD-peptidases. A vector has been constructed and introduced by electrotransformation in the original Actinomadura R39 strain, allowing high-level expression and secretion of the DD-peptidase/PBP (250 mg.l-1). The gene encoding the desired protein is processed differently in Actinomadura R39 and Streptomyces lividans. Incorrect processing in Streptomyces lividans leads to a secreted protein which is inert in terms of DD-peptidase activity and penicillin-binding capacity. |
| Databáze: | OpenAIRE |
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