Three-dimensional structure of moenomycin A. A potent inhibitor of penicillin-binding protein 1b

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Three-dimensional structure of moenomycin A--a potent inhibitor of penicillin-binding protein 1b.

The first three-dimensional structure of moenomycin A in aqueous solution based on NMR-derived distance constraints and molecular dynamics simulations is presented. The antibiotic moenomycin A was obtained from the FlavomycinR complex by ultrafiltration, chromatography on a DEAE-cellulose ion exchanger and reverse-phase chromatography in 98% purity. In contrast to the previously reported behavi...

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Functional characterization of penicillin-binding protein 1b from Streptococcus pneumoniae.

The widespread use of antibiotics has encouraged the development of drug resistance in pathogenic bacteria. In order to overcome this problem, the modification of existing antibiotics and/or the identification of targets for the design of new antibiotics is currently being undertaken. Bifunctional penicillin-binding proteins (PBPs) are membrane-associated molecules whose transpeptidase (TP) act...

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ژورنال

عنوان ژورنال: European Journal of Biochemistry

سال: 1998

ISSN: 0014-2956,1432-1033

DOI: 10.1046/j.1432-1327.1998.2520500.x