5Y50
Crystal structure of eukaryotic MATE transporter AtDTX14
Summary for 5Y50
| Entry DOI | 10.2210/pdb5y50/pdb |
| Descriptor | Protein DETOXIFICATION 14 (1 entity in total) |
| Functional Keywords | alpha helical, membrane protein |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Cellular location | Membrane ; Multi-pass membrane protein : Q9C994 |
| Total number of polymer chains | 1 |
| Total formula weight | 49544.00 |
| Authors | Miyauchi, H.,Kusakizako, T.,Nishizawa, T.,Ishitani, R.,Nureki, O. (deposition date: 2017-08-06, release date: 2017-12-06, Last modification date: 2023-11-22) |
| Primary citation | Miyauchi, H.,Moriyama, S.,Kusakizako, T.,Kumazaki, K.,Nakane, T.,Yamashita, K.,Hirata, K.,Dohmae, N.,Nishizawa, T.,Ito, K.,Miyaji, T.,Moriyama, Y.,Ishitani, R.,Nureki, O. Structural basis for xenobiotic extrusion by eukaryotic MATE transporter Nat Commun, 8:1633-1633, 2017 Cited by PubMed Abstract: Mulitidrug and toxic compound extrusion (MATE) family transporters export xenobiotics to maintain cellular homeostasis. The human MATE transporters mediate the excretion of xenobiotics and cationic clinical drugs, whereas some plant MATE transporters are responsible for aluminum tolerance and secondary metabolite transport. Here we report the crystal structure of the eukaryotic MATE transporter from Arabidopsis thaliana, at 2.6 Å resolution. The structure reveals that its carboxy-terminal lobe (C-lobe) contains an extensive hydrogen-bonding network with well-conserved acidic residues, and their importance is demonstrated by the structure-based mutational analysis. The structural and functional analyses suggest that the transport mechanism involves the structural change of transmembrane helix 7, induced by the formation of a hydrogen-bonding network upon the protonation of the conserved acidic residue in the C-lobe. Our findings provide insights into the transport mechanism of eukaryotic MATE transporters, which is important for the improvement of the pharmacokinetics of the clinical drugs. PubMed: 29158478DOI: 10.1038/s41467-017-01541-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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