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

Maria T. Rodolis; Agnes Mihalyi; Christian Ducho; Kornelia Eitel; Bertolt Gust; Rebecca J. M. Goss; Timothy D. H. Bugg

doi:10.1039/c4cc06516f

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

Maria T. Rodolis, Agnes Mihalyi, Christian Ducho, Kornelia Eitel, Bertolt Gust, Rebecca J. M. Goss, Timothy D. H. Bugg^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

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 phi X174 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.

Original language	English
Pages (from-to)	13023-13025
Number of pages	3
Journal	Chemical Communications
Volume	50
Issue number	86
DOIs	https://doi.org/10.1039/c4cc06516f
Publication status	Published - 2014

Keywords

ACETYLMURAMYL-PENTAPEPTIDE-TRANSLOCASE
BIOSYNTHETIC GENE-CLUSTER
CELL-WALL SYNTHESIS
BACTERIOPHAGE PHI-X174
ESCHERICHIA-COLI
MUREIDOMYCIN-A
IDENTIFICATION
INHIBITION
ANALOGS

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title = "Mechanism of action of the uridyl peptide antibiotics: an unexpected link to a protein-protein interaction site in translocase MraY",

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 phi X174 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.",

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author = "Rodolis, {Maria T.} and Agnes Mihalyi and Christian Ducho and Kornelia Eitel and Bertolt Gust and Goss, {Rebecca J. M.} and Bugg, {Timothy D. H.}",

year = "2014",

doi = "10.1039/c4cc06516f",

language = "English",

volume = "50",

pages = "13023--13025",

journal = "Chemical Communications",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

number = "86",

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TY - JOUR

T1 - Mechanism of action of the uridyl peptide antibiotics: an unexpected link to a protein-protein interaction site in translocase MraY

AU - Rodolis, Maria T.

AU - Mihalyi, Agnes

AU - Ducho, Christian

AU - Eitel, Kornelia

AU - Gust, Bertolt

AU - Goss, Rebecca J. M.

AU - Bugg, Timothy D. H.

PY - 2014

Y1 - 2014

N2 - 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 phi X174 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.

AB - 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 phi X174 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.

KW - ACETYLMURAMYL-PENTAPEPTIDE-TRANSLOCASE

KW - BIOSYNTHETIC GENE-CLUSTER

KW - CELL-WALL SYNTHESIS

KW - BACTERIOPHAGE PHI-X174

KW - ESCHERICHIA-COLI

KW - MUREIDOMYCIN-A

KW - IDENTIFICATION

KW - INHIBITION

KW - ANALOGS

U2 - 10.1039/c4cc06516f

DO - 10.1039/c4cc06516f

M3 - Article

SN - 1359-7345

VL - 50

SP - 13023

EP - 13025

JO - Chemical Communications

JF - Chemical Communications

IS - 86

ER -

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

Abstract

Keywords

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