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...
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Nature Portfolio
2017-11-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-017-01399-2 |
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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 |
collection | DOAJ |
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. |
first_indexed | 2024-12-21T09:33:58Z |
format | Article |
id | doaj.art-cea6897583ad4ebb8d8c7dd84cf36388 |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-12-21T09:33:58Z |
publishDate | 2017-11-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
spelling | doaj.art-cea6897583ad4ebb8d8c7dd84cf363882022-12-21T19:08:41ZengNature PortfolioNature Communications2041-17232017-11-018111110.1038/s41467-017-01399-2Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumanniiUi Okada0Eiki Yamashita1Arthur Neuberger2Mayu Morimoto3Hendrik W. van Veen4Satoshi Murakami5Department of Life Science, Tokyo Institute of TechnologyInstitute for Protein Research, Osaka UniversityDepartment of Pharmacology, University of CambridgeDepartment of Life Science, Tokyo Institute of TechnologyDepartment of Pharmacology, University of CambridgeDepartment of Life Science, Tokyo Institute of TechnologyThe 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.https://doi.org/10.1038/s41467-017-01399-2 |
spellingShingle | 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 Nature Communications |
title | 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_short | Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii |
title_sort | crystal structure of tripartite type abc transporter macb from acinetobacter baumannii |
url | https://doi.org/10.1038/s41467-017-01399-2 |
work_keys_str_mv | AT uiokada crystalstructureoftripartitetypeabctransportermacbfromacinetobacterbaumannii AT eikiyamashita crystalstructureoftripartitetypeabctransportermacbfromacinetobacterbaumannii AT arthurneuberger crystalstructureoftripartitetypeabctransportermacbfromacinetobacterbaumannii AT mayumorimoto crystalstructureoftripartitetypeabctransportermacbfromacinetobacterbaumannii AT hendrikwvanveen crystalstructureoftripartitetypeabctransportermacbfromacinetobacterbaumannii AT satoshimurakami crystalstructureoftripartitetypeabctransportermacbfromacinetobacterbaumannii |