Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 118, Issue 46, Pages -Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.2107335118
Keywords
membrane protein structure; multidrug resistance transporter; phylogenetic analysis
Categories
Funding
- Max Planck Society
- Center of Excellence (Macromolecular Complexes) Frank-furt
- International Academic Exchange Fund of the Graduate School of Tianjin University
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MATE transporters utilize H+ or Na+ gradients to export xenobiotics, with the substrate binding site located in the N bundle playing a crucial role in its function. The crystal structure of a MATE transporter from Aquifex aeolicus provides new insights into this important transporter family.
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-angstrom 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.
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