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

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.

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Autores principales:	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
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/5893b624e29f4e1b9969ad99f17cd15a
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spelling	oai:doaj.org-article:5893b624e29f4e1b9969ad99f17cd15a2021-12-02T14:35:44ZStructural insight into YcbB-mediated beta-lactam resistance in Escherichia coli10.1038/s41467-019-09507-02041-1723https://doaj.org/article/5893b624e29f4e1b9969ad99f17cd15a2019-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-09507-0https://doaj.org/toc/2041-1723In 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.Nathanael A. CaveneyGuillermo CaballeroHenri VoedtsAna NiciforovicLiam J. WorrallMarija VuckovicMatthieu FonvielleJean-Emmanuel HugonnetMichel ArthurNatalie C. J. StrynadkaNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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 Structural insight into YcbB-mediated beta-lactam resistance in Escherichia coli
description	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.
format	article
author	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
author_facet	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
author_sort	Nathanael A. Caveney
title	Structural insight into YcbB-mediated beta-lactam resistance in Escherichia coli
title_short	Structural insight into YcbB-mediated beta-lactam resistance in Escherichia coli
title_full	Structural insight into YcbB-mediated beta-lactam resistance in Escherichia coli
title_fullStr	Structural insight into YcbB-mediated beta-lactam resistance in Escherichia coli
title_full_unstemmed	Structural insight into YcbB-mediated beta-lactam resistance in Escherichia coli
title_sort	structural insight into ycbb-mediated beta-lactam resistance in escherichia coli
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/5893b624e29f4e1b9969ad99f17cd15a
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Structural insight into YcbB-mediated beta-lactam resistance in Escherichia coli

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