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• W2023954169 abstract "Methicillin-resistant Staphylococcus aureus (MRSA) has acquired a unique penicillin-binding protein (PBP), PBP 2a, which has rendered the organism resistant to the action of all available β-lactam antibiotics. The X-ray structure of PBP 2a shows the active site in a closed conformation, consistent with resistance to inhibition by β-lactam antibiotics. However, it is known that PBP 2a avidly cross-links the S. aureus cell wall, which is its physiological function. It is shown herein that synthetic fragments of the bacterial cell wall bind in a saturable manner to PBP 2a and cause a conformational change in the protein that makes the active site more accessible to binding to a β-lactam antibiotic. These observations and measurements point to a novel strategy by nature to keep the active site of PBP 2a sheltered from the inhibitory activity of the antibiotics, yet it becomes available to the polymeric cell wall by a requisite conformational change for the critical cell wall cross-linking reaction." @default.
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• W2023954169 date "2005-02-01" @default.
• W2023954169 modified "2023-10-17" @default.
• W2023954169 title "Activation for Catalysis of Penicillin-Binding Protein 2a from Methicillin-Resistant <i>Staphylococcus </i><i>a</i><i>ureus</i> by Bacterial Cell Wall" @default.
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• W2023954169 doi "https://doi.org/10.1021/ja0434376" @default.
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