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- W2317687692 abstract "The three-dimensional (3D) structure of bottromycin A2, a natural anti-methicillin-resistant Staphylococcus aureus (MRSA) and anti-vancomycin-resistant Enterococci (VRE) agent consisting of seven amino acids, has been investigated through NMR spectroscopy. On the basis of 57 experimental constraints, a total of 34 converged structures were obtained. The average pairwise atomic root mean square difference is 0.74±0.59 Å for all heavy atoms. The resulting structure indicates an interesting feature in that the three C-terminal residues of bottromycin A2 fold back on the 12-membered cyclic skeleton made by the four N-terminal residues. Thus, MePro(2) and Thia-β-Ala-OMe(7), modification of which significantly affects the antibacterial activities of bottromycin A2, are located on one side of its 3D structure. These distinct structural features might be important for the binding of bottromycin A2 with the bacterial ribosome." @default.
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- W2317687692 date "2012-01-01" @default.
- W2317687692 modified "2023-10-18" @default.
- W2317687692 title "Three-Dimensional Solution Structure of Bottromycin A2: A Potent Antibiotic Active against Methicillin-Resistant Staphylococcus aureus and Vancomycin-Resistant Enterococci" @default.
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- W2317687692 doi "https://doi.org/10.1248/cpb.60.169" @default.
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