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Issue 86, 2014
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Mechanism of action of the uridyl peptide antibiotics: an unexpected link to a protein–protein interaction site in translocase MraY

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Abstract

The pacidamycin and muraymycin uridyl peptide antibiotics show some structural resemblance to an Arg-Trp-x-x-Trp sequence motif for protein–protein interaction between bacteriophage ϕX174 protein E and E. coli translocase MraY. Members of the UPA class, and a synthetic uridine–peptide analogue, were found to show reduced levels of inhibition to F288L or E287A mutant MraY enzymes, implying that the UPAs interact at this extracellular site as part of the enzyme inhibition mechanism.

Graphical abstract: Mechanism of action of the uridyl peptide antibiotics: an unexpected link to a protein–protein interaction site in translocase MraY

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Publication details

The article was received on 19 Aug 2014, accepted on 09 Sep 2014 and first published on 09 Sep 2014


Article type: Communication
DOI: 10.1039/C4CC06516F
Citation: Chem. Commun., 2014,50, 13023-13025
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    Mechanism of action of the uridyl peptide antibiotics: an unexpected link to a protein–protein interaction site in translocase MraY

    M. T. Rodolis, A. Mihalyi, C. Ducho, K. Eitel, B. Gust, R. J. M. Goss and T. D. H. Bugg, Chem. Commun., 2014, 50, 13023
    DOI: 10.1039/C4CC06516F

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