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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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Rodolis, Maria T., Mihalyi, Agnes, Ducho, Christian, Eitel, Kornelia, Gust, Bertolt, Goss, Rebecca J. M. and Bugg, Tim (2014) Mechanism of action of the uridyl peptide antibiotics: an unexpected link to a protein–protein interaction site in translocase MraY. Chemical Communications, 50 (86). pp. 13023-13025. doi:10.1039/c4cc06516f ISSN 1359-7345.
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Official URL: http://dx.doi.org/10.1039/c4cc06516f
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.
Item Type: | Journal Article | ||||||||
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Subjects: | Q Science > QD Chemistry Q Science > QP Physiology R Medicine > RM Therapeutics. Pharmacology |
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry | ||||||||
Library of Congress Subject Headings (LCSH): | Anti-infective agents, Protein-protein interactions , Enzyme inhibitors | ||||||||
Journal or Publication Title: | Chemical Communications | ||||||||
Publisher: | Royal Society of Chemistry | ||||||||
ISSN: | 1359-7345 | ||||||||
Official Date: | 9 September 2014 | ||||||||
Dates: |
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Volume: | 50 | ||||||||
Number: | 86 | ||||||||
Page Range: | pp. 13023-13025 | ||||||||
DOI: | 10.1039/c4cc06516f | ||||||||
Status: | Peer Reviewed | ||||||||
Publication Status: | Published | ||||||||
Access rights to Published version: | Restricted or Subscription Access | ||||||||
Funder: | National Science Foundation (U.S.) (NSF) |
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