Structural and functional insights into esterase-mediated macrolide resistance

Erythromycin esterases (Eres) cleave the macrolactone ring of macrolides, a class of widely used antibiotics. Structures of EreC, in silico flexible docking studies and previous mutagenesis data lead to the proposal of a detailed catalytic mechanism for the Ere family of enzymes.

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Autores principales:	Michał Zieliński, Jaeok Park, Barry Sleno, Albert M. Berghuis
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/7b2d872b0cc04ef1b3ff7eb82c9ff6ed
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spelling	oai:doaj.org-article:7b2d872b0cc04ef1b3ff7eb82c9ff6ed2021-12-02T16:30:42ZStructural and functional insights into esterase-mediated macrolide resistance10.1038/s41467-021-22016-32041-1723https://doaj.org/article/7b2d872b0cc04ef1b3ff7eb82c9ff6ed2021-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-22016-3https://doaj.org/toc/2041-1723Erythromycin esterases (Eres) cleave the macrolactone ring of macrolides, a class of widely used antibiotics. Structures of EreC, in silico flexible docking studies and previous mutagenesis data lead to the proposal of a detailed catalytic mechanism for the Ere family of enzymes.Michał ZielińskiJaeok ParkBarry SlenoAlbert M. BerghuisNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-9 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Michał Zieliński Jaeok Park Barry Sleno Albert M. Berghuis Structural and functional insights into esterase-mediated macrolide resistance
description	Erythromycin esterases (Eres) cleave the macrolactone ring of macrolides, a class of widely used antibiotics. Structures of EreC, in silico flexible docking studies and previous mutagenesis data lead to the proposal of a detailed catalytic mechanism for the Ere family of enzymes.
format	article
author	Michał Zieliński Jaeok Park Barry Sleno Albert M. Berghuis
author_facet	Michał Zieliński Jaeok Park Barry Sleno Albert M. Berghuis
author_sort	Michał Zieliński
title	Structural and functional insights into esterase-mediated macrolide resistance
title_short	Structural and functional insights into esterase-mediated macrolide resistance
title_full	Structural and functional insights into esterase-mediated macrolide resistance
title_fullStr	Structural and functional insights into esterase-mediated macrolide resistance
title_full_unstemmed	Structural and functional insights into esterase-mediated macrolide resistance
title_sort	structural and functional insights into esterase-mediated macrolide resistance
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/7b2d872b0cc04ef1b3ff7eb82c9ff6ed
work_keys_str_mv	AT michałzielinski structuralandfunctionalinsightsintoesterasemediatedmacrolideresistance AT jaeokpark structuralandfunctionalinsightsintoesterasemediatedmacrolideresistance AT barrysleno structuralandfunctionalinsightsintoesterasemediatedmacrolideresistance AT albertmberghuis structuralandfunctionalinsightsintoesterasemediatedmacrolideresistance
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Structural and functional insights into esterase-mediated macrolide resistance

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