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Proc Natl Acad Sci U S A. 2008 Jan 15;105(2):431-6. doi: 10.1073/pnas.0710868105. Epub 2008 Jan 8.

Domain requirement of moenomycin binding to bifunctional transglycosylases and development of high-throughput discovery of antibiotics.

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1
Genomics Research Center, Academia Sinica, Sec. 2, 128 Academia Road, Nangang, Taipei 115, Taiwan.

Abstract

Moenomycin inhibits bacterial growth by blocking the transglycosylase activity of class A penicillin-binding proteins (PBPs), which are key enzymes in bacterial cell wall synthesis. We compared the binding affinities of moenomycin A with various truncated PBPs by using surface plasmon resonance analysis and found that the transmembrane domain is important for moenomycin binding. Full-length class A PBPs from 16 bacterial species were produced, and their binding activities showed a correlation with the antimicrobial activity of moenomycin against Enterococcus faecalis and Staphylococcus aureus. On the basis of these findings, a fluorescence anisotropy-based high-throughput assay was developed and used successfully for identification of transglycosylase inhibitors.

PMID:
18182485
PMCID:
PMC2206553
DOI:
10.1073/pnas.0710868105
[Indexed for MEDLINE]
Free PMC Article
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