mBio
(Apr 2021)
Cryo-EM Structures of CusA Reveal a Mechanism of Metal-Ion Export
Mitchell A. Moseng,
Meinan Lyu,
Tanadet Pipatpolkai,
Przemyslaw Glaza,
Corey C. Emerson,
Phoebe L. Stewart,
Phillip J. Stansfeld,
Edward W. Yu
Affiliations
Mitchell A. Moseng
Department of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA
Meinan Lyu
Department of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA
Tanadet Pipatpolkai
ORCiD Department of Biochemistry, University of Oxford, Oxford, United Kingdom
Przemyslaw Glaza
Department of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA
Corey C. Emerson
Department of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA
Phoebe L. Stewart
ORCiD Department of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA
Phillip J. Stansfeld
ORCiD School of Life Sciences & Department of Chemistry, University of Warwick, Coventry, United Kingdom
Edward W. Yu
ORCiD Department of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA
DOI
https://doi.org/10.1128/mBio.00452-21
Journal volume & issue
Vol. 12,
no. 2
Abstract
Read online
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.
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