Journal
TRENDS IN MICROBIOLOGY
Volume 11, Issue 4, Pages 145-148Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/S0966-842X(03)00046-5
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Funding
- NIAID NIH HHS [AI 46610] Funding Source: Medline
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Class resistance to beta-lactam antibiotics in Gram-positive bacteria is mediated by structural changes in transpeptidase penicillin-binding proteins. These structural changes render a complex series of interactions between antibiotic and protein that are energetically unfavorable, such that the active site is inactivated not at all or too slowly to prevent cell-wall synthesis and bacterial growth. Determination of the crystal structure of the low-affinity penicillin-binding protein PBP2a, which mediates beta-lactam antibiotic resistance in staphylococci, has identified the molecular structures and interactions that are responsible for resistance. This information could be useful for designing beta-lactams to overcome these structural impediments, as well as resistance.
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