7KF5

Cryo-electron microscopy structure of the heavy metal efflux pump CusA in the symmetric closed state

7KF5 の概要

• エントリーDOI: 10.2210/pdb7kf5/pdb
• EMDBエントリー: 22843
• 分子名称: Cation efflux system protein CusA (1 entity in total)
• 機能のキーワード: efflux, pump, heavy metal. copper, silver, closed, open, transport, membrane protein, transport protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 347501.84

構造登録者

Moseng, M.A. (登録日: 2020-10-13, 公開日: 2021-04-14, 最終更新日: 2024-03-06)

主引用文献

Moseng, M.A.,Lyu, M.,Pipatpolkai, T.,Glaza, P.,Emerson, C.C.,Stewart, P.L.,Stansfeld, P.J.,Yu, E.W.
Cryo-EM Structures of CusA Reveal a Mechanism of Metal-Ion Export.
Mbio, 12:-, 2021

PubMed 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.

PubMed: 33820823
DOI: 10.1128/mBio.00452-21

実験手法

ELECTRON MICROSCOPY (3.2 Å)