Site-directed mutagenesis of the mecA gene from a methicillin-resistant strain of Staphylococcus aureus
| Autor: | C. Y. E. Wu, Paul L. Skatrud, Larry C. Blaszczak, Serhat Ünal, J. E. Flokowitsch, William E. Alborn, JoAnn Hoskins, David A. Preston |
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| Rok vydání: | 1994 |
| Předmět: |
Staphylococcus aureus
Glycosylation Penicillin binding proteins DNA Mutational Analysis Molecular Sequence Data Penicillins Muramoylpentapeptide Carboxypeptidase Biology medicine.disease_cause Binding Competitive Microbiology Bacterial Proteins polycyclic compounds medicine Penicillin-Binding Proteins Amino Acid Sequence Site-directed mutagenesis Molecular Biology Peptide sequence Conserved Sequence Antibacterial agent Base Sequence SCCmec Membrane Proteins Protein Structure Tertiary Penicillin Transmembrane domain Cefamandole Hexosyltransferases Peptidyl Transferases Mutagenesis Site-Directed Methicillin Resistance Carrier Proteins Research Article medicine.drug |
| Zdroj: | Journal of Bacteriology. 176:443-449 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.176.2.443-449.1994 |
| Popis: | The mecA-27r gene from Staphylococcus aureus 27r encodes penicillin-binding protein 2a (PBP2a-27r), which causes this strain to be methicillin resistant. Removal or replacement of the N-terminal transmembrane domain had no effect on binding of penicillin, but removal of portions of the putative transglycosylase domain (144, 245, or 341 amino acids after the transmembrane region) destroyed penicillin-binding activity. The SXXK, SXN, and KSG motifs, present in all penicillin-interacting enzymes, were found in the expected linear spatial arrangement within the putative transpeptidase region of PBP2a-27r. Alterations of amino acids in all three of these motifs resulted in elimination of penicillin-binding activity, confirming their roles in the interaction with penicillin. |
| Databáze: | OpenAIRE |
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