Cryo-EM Structures of CusA Reveal a Mechanism of Metal-Ion Export

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 tr...

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Autores principales: Mitchell A. Moseng, Meinan Lyu, Tanadet Pipatpolkai, Przemyslaw Glaza, Corey C. Emerson, Phoebe L. Stewart, Phillip J. Stansfeld, Edward W. Yu
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Lenguaje:EN
Publicado: American Society for Microbiology 2021
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Acceso en línea:https://doaj.org/article/d5623e1c81b943f792bc80254cdda644
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spelling oai:doaj.org-article:d5623e1c81b943f792bc80254cdda6442021-11-03T18:56:09ZCryo-EM Structures of CusA Reveal a Mechanism of Metal-Ion Export2150-751110.1128/mBio.00452-21https://doaj.org/article/d5623e1c81b943f792bc80254cdda6442021-04-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.00452-21https://doaj.org/toc/2150-7511 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.Mitchell A. MosengMeinan LyuTanadet PipatpolkaiPrzemyslaw GlazaCorey C. EmersonPhoebe L. StewartPhillip J. StansfeldEdward W. YuAmerican Society for MicrobiologyarticleMicrobiologyQR1-502ENmBio, Vol 12, Iss 2 (2021)
institution DOAJ
collection DOAJ
language EN
topic Microbiology
QR1-502
spellingShingle Microbiology
QR1-502
Mitchell A. Moseng
Meinan Lyu
Tanadet Pipatpolkai
Przemyslaw Glaza
Corey C. Emerson
Phoebe L. Stewart
Phillip J. Stansfeld
Edward W. Yu
Cryo-EM Structures of CusA Reveal a Mechanism of Metal-Ion Export
description 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.
format article
author Mitchell A. Moseng
Meinan Lyu
Tanadet Pipatpolkai
Przemyslaw Glaza
Corey C. Emerson
Phoebe L. Stewart
Phillip J. Stansfeld
Edward W. Yu
author_facet Mitchell A. Moseng
Meinan Lyu
Tanadet Pipatpolkai
Przemyslaw Glaza
Corey C. Emerson
Phoebe L. Stewart
Phillip J. Stansfeld
Edward W. Yu
author_sort Mitchell A. Moseng
title Cryo-EM Structures of CusA Reveal a Mechanism of Metal-Ion Export
title_short Cryo-EM Structures of CusA Reveal a Mechanism of Metal-Ion Export
title_full Cryo-EM Structures of CusA Reveal a Mechanism of Metal-Ion Export
title_fullStr Cryo-EM Structures of CusA Reveal a Mechanism of Metal-Ion Export
title_full_unstemmed Cryo-EM Structures of CusA Reveal a Mechanism of Metal-Ion Export
title_sort cryo-em structures of cusa reveal a mechanism of metal-ion export
publisher American Society for Microbiology
publishDate 2021
url https://doaj.org/article/d5623e1c81b943f792bc80254cdda644
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AT tanadetpipatpolkai cryoemstructuresofcusarevealamechanismofmetalionexport
AT przemyslawglaza cryoemstructuresofcusarevealamechanismofmetalionexport
AT coreycemerson cryoemstructuresofcusarevealamechanismofmetalionexport
AT phoebelstewart cryoemstructuresofcusarevealamechanismofmetalionexport
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