Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii

The tripartite multidrug efflux pump MacA-MacB-TolC in Gram-negative bacterial pathogens is driven by the ATPase MacB, which belongs to the ATP-binding cassette (ABC) superfamily. Here the authors present the 3.4 Å resolution crystal structure of MacB, and compare it with other known ABC transporter...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Ui Okada, Eiki Yamashita, Arthur Neuberger, Mayu Morimoto, Hendrik W. van Veen, Satoshi Murakami
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2017
Materias:
Q
Acceso en línea:https://doaj.org/article/cea6897583ad4ebb8d8c7dd84cf36388
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:cea6897583ad4ebb8d8c7dd84cf36388
record_format dspace
spelling oai:doaj.org-article:cea6897583ad4ebb8d8c7dd84cf363882021-12-02T15:37:06ZCrystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii10.1038/s41467-017-01399-22041-1723https://doaj.org/article/cea6897583ad4ebb8d8c7dd84cf363882017-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-01399-2https://doaj.org/toc/2041-1723The tripartite multidrug efflux pump MacA-MacB-TolC in Gram-negative bacterial pathogens is driven by the ATPase MacB, which belongs to the ATP-binding cassette (ABC) superfamily. Here the authors present the 3.4 Å resolution crystal structure of MacB, and compare it with other known ABC transporter structures.Ui OkadaEiki YamashitaArthur NeubergerMayu MorimotoHendrik W. van VeenSatoshi MurakamiNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-11 (2017)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Ui Okada
Eiki Yamashita
Arthur Neuberger
Mayu Morimoto
Hendrik W. van Veen
Satoshi Murakami
Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii
description The tripartite multidrug efflux pump MacA-MacB-TolC in Gram-negative bacterial pathogens is driven by the ATPase MacB, which belongs to the ATP-binding cassette (ABC) superfamily. Here the authors present the 3.4 Å resolution crystal structure of MacB, and compare it with other known ABC transporter structures.
format article
author Ui Okada
Eiki Yamashita
Arthur Neuberger
Mayu Morimoto
Hendrik W. van Veen
Satoshi Murakami
author_facet Ui Okada
Eiki Yamashita
Arthur Neuberger
Mayu Morimoto
Hendrik W. van Veen
Satoshi Murakami
author_sort Ui Okada
title Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii
title_short Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii
title_full Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii
title_fullStr Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii
title_full_unstemmed Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii
title_sort crystal structure of tripartite-type abc transporter macb from acinetobacter baumannii
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/cea6897583ad4ebb8d8c7dd84cf36388
work_keys_str_mv AT uiokada crystalstructureoftripartitetypeabctransportermacbfromacinetobacterbaumannii
AT eikiyamashita crystalstructureoftripartitetypeabctransportermacbfromacinetobacterbaumannii
AT arthurneuberger crystalstructureoftripartitetypeabctransportermacbfromacinetobacterbaumannii
AT mayumorimoto crystalstructureoftripartitetypeabctransportermacbfromacinetobacterbaumannii
AT hendrikwvanveen crystalstructureoftripartitetypeabctransportermacbfromacinetobacterbaumannii
AT satoshimurakami crystalstructureoftripartitetypeabctransportermacbfromacinetobacterbaumannii
_version_ 1718386260152680448