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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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Article information


Submitted
19 Aug 2014
Accepted
09 Sep 2014
First published
09 Sep 2014

Chem. Commun., 2014,50, 13023-13025
Article type
Communication

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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