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

Ui Okada; Eiki Yamashita; Arthur Neuberger; Mayu Morimoto; Hendrik W. van Veen; Satoshi Murakami

doi:10.1038/s41467-017-01399-2

Nature Communications (Nov 2017)

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

Ui Okada,
Eiki Yamashita,
Arthur Neuberger,
Mayu Morimoto,
Hendrik W. van Veen,
Satoshi Murakami

Affiliations

Ui Okada: Department of Life Science, Tokyo Institute of Technology
Eiki Yamashita: Institute for Protein Research, Osaka University
Arthur Neuberger: Department of Pharmacology, University of Cambridge
Mayu Morimoto: Department of Life Science, Tokyo Institute of Technology
Hendrik W. van Veen: Department of Pharmacology, University of Cambridge
Satoshi Murakami: Department of Life Science, Tokyo Institute of Technology

DOI: https://doi.org/10.1038/s41467-017-01399-2
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 11

Abstract

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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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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