5Y50

Crystal structure of eukaryotic MATE transporter AtDTX14

5Y50 の概要

• エントリーDOI: 10.2210/pdb5y50/pdb
• 分子名称: Protein DETOXIFICATION 14 (1 entity in total)
• 機能のキーワード: alpha helical, membrane protein
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• 細胞内の位置: Membrane ; Multi-pass membrane protein : Q9C994
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 49544.00

構造登録者

Miyauchi, H.,Kusakizako, T.,Nishizawa, T.,Ishitani, R.,Nureki, O. (登録日: 2017-08-06, 公開日: 2017-12-06, 最終更新日: 2023-11-22)

主引用文献

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

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: 29158478
DOI: 10.1038/s41467-017-01541-0

実験手法

X-RAY DIFFRACTION (2.6 Å)