Allosteric drug transport mechanism of multidrug transporter AcrB

Gram-negative bacteria can display intrinsic antibiotic resistance due to the action of tripartite efflux pumps, which include a H+/drug antiporter component. Here, the authors present a structure-function analysis of antiporter AcrB in intermediate states of the transport cycle, showing novel drug-...

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Autores principales:	Heng-Keat Tam, Wuen Ee Foong, Christine Oswald, Andrea Herrmann, Hui Zeng, Klaas M. Pos
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/6482f47ba7254e868df9dbcc9afdc705
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id	oai:doaj.org-article:6482f47ba7254e868df9dbcc9afdc705
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spelling	oai:doaj.org-article:6482f47ba7254e868df9dbcc9afdc7052021-12-02T16:31:58ZAllosteric drug transport mechanism of multidrug transporter AcrB10.1038/s41467-021-24151-32041-1723https://doaj.org/article/6482f47ba7254e868df9dbcc9afdc7052021-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-24151-3https://doaj.org/toc/2041-1723Gram-negative bacteria can display intrinsic antibiotic resistance due to the action of tripartite efflux pumps, which include a H+/drug antiporter component. Here, the authors present a structure-function analysis of antiporter AcrB in intermediate states of the transport cycle, showing novel drug-binding sites and transport pathways.Heng-Keat TamWuen Ee FoongChristine OswaldAndrea HerrmannHui ZengKlaas M. PosNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Heng-Keat Tam Wuen Ee Foong Christine Oswald Andrea Herrmann Hui Zeng Klaas M. Pos Allosteric drug transport mechanism of multidrug transporter AcrB
description	Gram-negative bacteria can display intrinsic antibiotic resistance due to the action of tripartite efflux pumps, which include a H+/drug antiporter component. Here, the authors present a structure-function analysis of antiporter AcrB in intermediate states of the transport cycle, showing novel drug-binding sites and transport pathways.
format	article
author	Heng-Keat Tam Wuen Ee Foong Christine Oswald Andrea Herrmann Hui Zeng Klaas M. Pos
author_facet	Heng-Keat Tam Wuen Ee Foong Christine Oswald Andrea Herrmann Hui Zeng Klaas M. Pos
author_sort	Heng-Keat Tam
title	Allosteric drug transport mechanism of multidrug transporter AcrB
title_short	Allosteric drug transport mechanism of multidrug transporter AcrB
title_full	Allosteric drug transport mechanism of multidrug transporter AcrB
title_fullStr	Allosteric drug transport mechanism of multidrug transporter AcrB
title_full_unstemmed	Allosteric drug transport mechanism of multidrug transporter AcrB
title_sort	allosteric drug transport mechanism of multidrug transporter acrb
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/6482f47ba7254e868df9dbcc9afdc705
work_keys_str_mv	AT hengkeattam allostericdrugtransportmechanismofmultidrugtransporteracrb AT wueneefoong allostericdrugtransportmechanismofmultidrugtransporteracrb AT christineoswald allostericdrugtransportmechanismofmultidrugtransporteracrb AT andreaherrmann allostericdrugtransportmechanismofmultidrugtransporteracrb AT huizeng allostericdrugtransportmechanismofmultidrugtransporteracrb AT klaasmpos allostericdrugtransportmechanismofmultidrugtransporteracrb
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Allosteric drug transport mechanism of multidrug transporter AcrB

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