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Structure of the MacAB-TolC ABC-type tripartite multidrug efflux pump
The MacA-MacB-TolC assembly of Escherichia coli is a transmembrane machine that spans the cell envelope and actively extrudes substrates, including macrolide antibiotics and polypeptide virulence factors. These transport processes are energized by the ATPase MacB, a member of the ATP-binding cassett...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2017
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5447821/ https://www.ncbi.nlm.nih.gov/pubmed/28504659 http://dx.doi.org/10.1038/nmicrobiol.2017.70 |
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author | Fitzpatrick, Anthony W.P. Llabrés, Salomé Neuberger, Arthur Blaza, James N. Bai, Xiao-chen Okada, Ui Murakami, Satoshi van Veen, Hendrik W. Zachariae, Ulrich Scheres, Sjors H.W. Luisi, Ben F. Du, Dijun |
author_facet | Fitzpatrick, Anthony W.P. Llabrés, Salomé Neuberger, Arthur Blaza, James N. Bai, Xiao-chen Okada, Ui Murakami, Satoshi van Veen, Hendrik W. Zachariae, Ulrich Scheres, Sjors H.W. Luisi, Ben F. Du, Dijun |
author_sort | Fitzpatrick, Anthony W.P. |
collection | PubMed |
description | The MacA-MacB-TolC assembly of Escherichia coli is a transmembrane machine that spans the cell envelope and actively extrudes substrates, including macrolide antibiotics and polypeptide virulence factors. These transport processes are energized by the ATPase MacB, a member of the ATP-binding cassette (ABC) superfamily. We present an electron cryo-microscopy structure of the ABC-type tripartite assembly at near-atomic resolution. A hexamer of the periplasmic protein MacA bridges between a TolC trimer in the outer membrane and a MacB dimer in the inner membrane, generating a quaternary structure with a central channel for substrate translocation. A gating ring found in MacA is proposed to act as a one-way valve in substrate transport. The MacB structure features an atypical transmembrane domain (TMD) with a closely packed dimer interface and a periplasmic opening that is the likely portal for substrate entry from the periplasm, with subsequent displacement through an allosteric transport mechanism. |
format | Online Article Text |
id | pubmed-5447821 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
record_format | MEDLINE/PubMed |
spelling | pubmed-54478212017-11-15 Structure of the MacAB-TolC ABC-type tripartite multidrug efflux pump Fitzpatrick, Anthony W.P. Llabrés, Salomé Neuberger, Arthur Blaza, James N. Bai, Xiao-chen Okada, Ui Murakami, Satoshi van Veen, Hendrik W. Zachariae, Ulrich Scheres, Sjors H.W. Luisi, Ben F. Du, Dijun Nat Microbiol Article The MacA-MacB-TolC assembly of Escherichia coli is a transmembrane machine that spans the cell envelope and actively extrudes substrates, including macrolide antibiotics and polypeptide virulence factors. These transport processes are energized by the ATPase MacB, a member of the ATP-binding cassette (ABC) superfamily. We present an electron cryo-microscopy structure of the ABC-type tripartite assembly at near-atomic resolution. A hexamer of the periplasmic protein MacA bridges between a TolC trimer in the outer membrane and a MacB dimer in the inner membrane, generating a quaternary structure with a central channel for substrate translocation. A gating ring found in MacA is proposed to act as a one-way valve in substrate transport. The MacB structure features an atypical transmembrane domain (TMD) with a closely packed dimer interface and a periplasmic opening that is the likely portal for substrate entry from the periplasm, with subsequent displacement through an allosteric transport mechanism. 2017-05-15 /pmc/articles/PMC5447821/ /pubmed/28504659 http://dx.doi.org/10.1038/nmicrobiol.2017.70 Text en Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article Fitzpatrick, Anthony W.P. Llabrés, Salomé Neuberger, Arthur Blaza, James N. Bai, Xiao-chen Okada, Ui Murakami, Satoshi van Veen, Hendrik W. Zachariae, Ulrich Scheres, Sjors H.W. Luisi, Ben F. Du, Dijun Structure of the MacAB-TolC ABC-type tripartite multidrug efflux pump |
title | Structure of the MacAB-TolC ABC-type tripartite multidrug efflux pump |
title_full | Structure of the MacAB-TolC ABC-type tripartite multidrug efflux pump |
title_fullStr | Structure of the MacAB-TolC ABC-type tripartite multidrug efflux pump |
title_full_unstemmed | Structure of the MacAB-TolC ABC-type tripartite multidrug efflux pump |
title_short | Structure of the MacAB-TolC ABC-type tripartite multidrug efflux pump |
title_sort | structure of the macab-tolc abc-type tripartite multidrug efflux pump |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5447821/ https://www.ncbi.nlm.nih.gov/pubmed/28504659 http://dx.doi.org/10.1038/nmicrobiol.2017.70 |
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