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Bacterial Metal Resistance: Coping with Copper without Cooperativity?

In Escherichia coli and other Gram-negative bacteria, tripartite efflux pumps (TEPs) span the entire cell envelope and serve to remove noxious molecules from the cell. CusBCA is a TEP responsible for copper and silver detoxification in E. coli powered by the resistance-nodulation-cell division (RND)...

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Autores principales: Greene, Nicholas P., Koronakis, Vassilis
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Microbiology 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8262934/
https://www.ncbi.nlm.nih.gov/pubmed/34126768
http://dx.doi.org/10.1128/mBio.00653-21
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author Greene, Nicholas P.
Koronakis, Vassilis
author_facet Greene, Nicholas P.
Koronakis, Vassilis
author_sort Greene, Nicholas P.
collection PubMed
description In Escherichia coli and other Gram-negative bacteria, tripartite efflux pumps (TEPs) span the entire cell envelope and serve to remove noxious molecules from the cell. CusBCA is a TEP responsible for copper and silver detoxification in E. coli powered by the resistance-nodulation-cell division (RND) transporter, CusA. In a recent study, Moseng et al. (M. A. Moseng, M. Lyu, T. Pipatpolkai, P. Glaza, et al., mBio 12:e00452-21, 2021, https://dx.doi.org/10.1128/mBio.00452-21) obtained cryo-electron microscopy (cryo-EM) structures of CusA trimers in the presence of copper. The multiple conformations revealed suggest that the three monomers function independently within the CusA trimer, contrary to the cooperative mechanism proposed for the multidrug exporting RND transporter, AcrB. The work prompts consideration of the mechanism of this class of transporter and provides a basis to underpin further studies of TEPs important for bacterial survival.
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spelling pubmed-82629342021-07-23 Bacterial Metal Resistance: Coping with Copper without Cooperativity? Greene, Nicholas P. Koronakis, Vassilis mBio Commentary In Escherichia coli and other Gram-negative bacteria, tripartite efflux pumps (TEPs) span the entire cell envelope and serve to remove noxious molecules from the cell. CusBCA is a TEP responsible for copper and silver detoxification in E. coli powered by the resistance-nodulation-cell division (RND) transporter, CusA. In a recent study, Moseng et al. (M. A. Moseng, M. Lyu, T. Pipatpolkai, P. Glaza, et al., mBio 12:e00452-21, 2021, https://dx.doi.org/10.1128/mBio.00452-21) obtained cryo-electron microscopy (cryo-EM) structures of CusA trimers in the presence of copper. The multiple conformations revealed suggest that the three monomers function independently within the CusA trimer, contrary to the cooperative mechanism proposed for the multidrug exporting RND transporter, AcrB. The work prompts consideration of the mechanism of this class of transporter and provides a basis to underpin further studies of TEPs important for bacterial survival. American Society for Microbiology 2021-06-15 /pmc/articles/PMC8262934/ /pubmed/34126768 http://dx.doi.org/10.1128/mBio.00653-21 Text en Copyright © 2021 Greene and Koronakis. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Commentary
Greene, Nicholas P.
Koronakis, Vassilis
Bacterial Metal Resistance: Coping with Copper without Cooperativity?
title Bacterial Metal Resistance: Coping with Copper without Cooperativity?
title_full Bacterial Metal Resistance: Coping with Copper without Cooperativity?
title_fullStr Bacterial Metal Resistance: Coping with Copper without Cooperativity?
title_full_unstemmed Bacterial Metal Resistance: Coping with Copper without Cooperativity?
title_short Bacterial Metal Resistance: Coping with Copper without Cooperativity?
title_sort bacterial metal resistance: coping with copper without cooperativity?
topic Commentary
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8262934/
https://www.ncbi.nlm.nih.gov/pubmed/34126768
http://dx.doi.org/10.1128/mBio.00653-21
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