Structural insight into YcbB-mediated beta-lactam resistance in Escherichia coli

Nathanael A. Caveney; Guillermo Caballero; Henri Voedts; Ana Niciforovic; Liam J. Worrall; Marija Vuckovic; Matthieu Fonvielle; Jean-Emmanuel Hugonnet; Michel Arthur; Natalie C. J. Strynadka

doi:10.1038/s41467-019-09507-0

Nature Communications (Apr 2019)

Structural insight into YcbB-mediated beta-lactam resistance in Escherichia coli

Nathanael A. Caveney,
Guillermo Caballero,
Henri Voedts,
Ana Niciforovic,
Liam J. Worrall,
Marija Vuckovic,
Matthieu Fonvielle,
Jean-Emmanuel Hugonnet,
Michel Arthur,
Natalie C. J. Strynadka

Affiliations

Nathanael A. Caveney: Department of Biochemistry and Molecular Biology and the Centre for Blood Research, University of British Columbia
Guillermo Caballero: Department of Biochemistry and Molecular Biology and the Centre for Blood Research, University of British Columbia
Henri Voedts: Sorbonne Université, Sorbonne Paris Cité, Université Paris Descartes, Université Paris Diderot, INSERM, Centre de Recherche des Cordeliers, CRC
Ana Niciforovic: Department of Biochemistry and Molecular Biology and the Centre for Blood Research, University of British Columbia
Liam J. Worrall: Department of Biochemistry and Molecular Biology and the Centre for Blood Research, University of British Columbia
Marija Vuckovic: Department of Biochemistry and Molecular Biology and the Centre for Blood Research, University of British Columbia
Matthieu Fonvielle: Sorbonne Université, Sorbonne Paris Cité, Université Paris Descartes, Université Paris Diderot, INSERM, Centre de Recherche des Cordeliers, CRC
Jean-Emmanuel Hugonnet: Sorbonne Université, Sorbonne Paris Cité, Université Paris Descartes, Université Paris Diderot, INSERM, Centre de Recherche des Cordeliers, CRC
Michel Arthur: Sorbonne Université, Sorbonne Paris Cité, Université Paris Descartes, Université Paris Diderot, INSERM, Centre de Recherche des Cordeliers, CRC
Natalie C. J. Strynadka: Department of Biochemistry and Molecular Biology and the Centre for Blood Research, University of British Columbia

DOI: https://doi.org/10.1038/s41467-019-09507-0
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 11

Abstract

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In E. coli, alternate peptidoglycan crosslinking reactions carried out by the L,D-transpeptidase YcbB can lead to beta-lactam resistance. Here, Caveney et al. solve the crystal structure of YcbB and shed light into its mechanism of action and into YcbB-mediated antibiotic resistance.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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