The structure of the Aquifex aeolicus MATE family multidrug resistance 
transporter and sequence comparisons suggest the existence of a new subfamily

Zhao, Jiangfeng; Xie, Hao; Mehdipour, Ahmad Reza; Safarian, Schara; Ermler, Ulrich; Münke, Cornelia; Thielmann, Yvonne; Hummer, Gerhard; Ebersberger, Ingo; Wang, Jingkang; Michel, Hartmut

doi:10.1073/pnas.2107335118

アイテム詳細

登録内容を編集ファイル形式で保存

一時保存へ追加

タグ情報を表示リリース履歴を表示詳細要約

公開

学術論文

The structure of the Aquifex aeolicus MATE family multidrug resistance transporter and sequence comparisons suggest the existence of a new subfamily

MPS-Authors

/persons/resource/persons267222

Zhao, Jiangfeng
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;
State Key Laboratory for Chemical Engineering, Collaborative Innovation Center of Chemical Science and Chemical Engineering, School of Chemical Engineering and Technology, Tianjin University, 300072 Tianjin, P. R. China;

/persons/resource/persons137954

Xie, Hao
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons146403

Mehdipour, Ahmad Reza
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137866

Safarian, Schara
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137648

Ermler, Ulrich
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137814

Münke, Cornelia
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137918

Thielmann, Yvonne
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons15259

Hummer, Gerhard
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137800

Michel, Hartmut
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

External Resource

There are no locators available

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

フルテキスト (公開)

公開されているフルテキストはありません

付随資料 (公開)

There is no public supplementary material available

引用

Zhao, J., Xie, H., Mehdipour, A. R., Safarian, S., Ermler, U., Münke, C., Thielmann, Y., Hummer, G., Ebersberger, I., Wang, J., & Michel, H. (2021). The structure of the Aquifex aeolicus MATE family multidrug resistance transporter and sequence comparisons suggest the existence of a new subfamily. Proceedings of the National Academy of Sciences of the United States of America, 118(46):. doi:10.1073/pnas.2107335118.

引用: https://hdl.handle.net/21.11116/0000-0009-7740-9

要旨

Multidrug and toxic compound extrusion (MATE) transporters are widespread in all domains of life. Bacterial MATE transporters confer multidrug resistance by utilizing an electrochemical gradient of H⁺ or Na⁺ to export xenobiotics across the membrane. Despite the availability of X-ray structures of several MATE transporters, a detailed understanding of the transport mechanism has remained elusive. Here we report the crystal structure of a MATE transporter from Aquifex aeolicus at 2.0-Å resolution. In light of its phylogenetic placement outside of the diversity of hitherto-described MATE transporters and the lack of conserved acidic residues, this protein may represent a subfamily of prokaryotic MATE transporters, which was proven by phylogenetic analysis. Furthermore, the crystal structure and substrate docking results indicate that the substrate binding site is located in the N bundle. The importance of residues surrounding this binding site was demonstrated by structure-based site-directed mutagenesis. We suggest that Aq_128 is functionally similar but structurally diverse from DinF subfamily transporters. Our results provide structural insights into the MATE transporter, which further advances our global understanding of this important transporter family.