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Cryo-EM structures of CusA reveal a mechanism of metal-ion export
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Moseng, Mitchell A., Lyu, Meinan, Pipatpolkai, Tanadet, Glaza, Przemyslaw, Emerson, Corey C., Stewart, Phoebe L., Stansfeld, Phillip J. and Yu, Edward W. (2021) Cryo-EM structures of CusA reveal a mechanism of metal-ion export. mBio, 12 (2). e00452-21. doi:10.1128/mBio.00452-21 ISSN 2150-7511.
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WRAP-Cryo-EM-structures-CusA-reveal-mechanism-metal-Ion-2021.pdf - Published Version - Requires a PDF viewer. Available under License Creative Commons Attribution 4.0. Download (6Mb) | Preview |
Official URL: https://doi.org/10.1128/mBio.00452-21
Abstract
Gram-negative bacteria utilize the resistance-nodulation-cell division (RND) superfamily of efflux pumps to expel a variety of toxic compounds from the cell. The CusA membrane protein, which recognizes and extrudes biocidal Cu(I) and Ag(I) ions, belongs to the heavy-metal efflux (HME) subfamily of RND efflux pumps. We here report four structures of the trimeric CusA heavy-metal efflux pump in the presence of Cu(I) using single-particle cryo-electron microscopy (cryo-EM). We discover that different CusA protomers within the trimer are able to bind Cu(I) ions simultaneously. Our structural data combined with molecular dynamics (MD) simulations allow us to propose a mechanism for ion transport where each CusA protomer functions independently within the trimer. The bacterial RND superfamily of efflux pumps mediate resistance to a variety of biocides, including Cu(I) and Ag(I) ions. Here we report four cryo-EM structures of the trimeric CusA pump in the presence of Cu(I). Combined with MD simulations, our data indicate that each CusA protomer within the trimer recognizes and extrudes Cu(I) independently. [Abstract copyright: Copyright © 2021 Moseng et al.]
Item Type: | Journal Article | ||||||||||||||||||||||||||||||||||||
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Subjects: | Q Science > QP Physiology Q Science > QR Microbiology |
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) Faculty of Science, Engineering and Medicine > Science > Chemistry > Computational and Theoretical Chemistry Centre |
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SWORD Depositor: | Library Publications Router | ||||||||||||||||||||||||||||||||||||
Library of Congress Subject Headings (LCSH): | Drug resistance in microorganisms, Gram-negative bacteria , Escherichia coli -- Effect of drugs on, Metal ions -- Metabolism, Electron microscopy | ||||||||||||||||||||||||||||||||||||
Journal or Publication Title: | mBio | ||||||||||||||||||||||||||||||||||||
Publisher: | American Society for Microbiology | ||||||||||||||||||||||||||||||||||||
ISSN: | 2150-7511 | ||||||||||||||||||||||||||||||||||||
Official Date: | 5 April 2021 | ||||||||||||||||||||||||||||||||||||
Dates: |
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Volume: | 12 | ||||||||||||||||||||||||||||||||||||
Number: | 2 | ||||||||||||||||||||||||||||||||||||
Article Number: | e00452-21 | ||||||||||||||||||||||||||||||||||||
DOI: | 10.1128/mBio.00452-21 | ||||||||||||||||||||||||||||||||||||
Status: | Peer Reviewed | ||||||||||||||||||||||||||||||||||||
Publication Status: | Published | ||||||||||||||||||||||||||||||||||||
Reuse Statement (publisher, data, author rights): | ** From PubMed via Jisc Publications Router | ||||||||||||||||||||||||||||||||||||
Access rights to Published version: | Open Access (Creative Commons) | ||||||||||||||||||||||||||||||||||||
Date of first compliant deposit: | 4 May 2021 | ||||||||||||||||||||||||||||||||||||
Date of first compliant Open Access: | 5 May 2021 | ||||||||||||||||||||||||||||||||||||
RIOXX Funder/Project Grant: |
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