Structural basis for xenobiotic extrusion by eukaryotic MATE transporter
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 second...
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| Vydáno v: | Nature communications Ročník 8; číslo 1; s. 1633 - 11 |
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| Hlavní autoři: | , , , , , , , , , , , , , |
| Médium: | Journal Article |
| Jazyk: | angličtina |
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Nature Publishing Group UK
21.11.2017
Nature Publishing Group Nature Portfolio |
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| ISSN: | 2041-1723, 2041-1723 |
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| 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.
Mulitidrug and toxic compound extrusion (MATE) family transporters export xenobiotics and some plant MATE transporters are involved in secondary metabolite transport. Here, the authors present the structure of the
Arabidopsis thaliana
MATE transporter AtDTX14 and propose a model for eukaryotic MATE transport mechanism. |
|---|---|
| AbstractList | 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.
Mulitidrug and toxic compound extrusion (MATE) family transporters export xenobiotics and some plant MATE transporters are involved in secondary metabolite transport. Here, the authors present the structure of the
Arabidopsis thaliana
MATE transporter AtDTX14 and propose a model for eukaryotic MATE transport mechanism. 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. Mulitidrug and toxic compound extrusion (MATE) family transporters export xenobiotics and some plant MATE transporters are involved in secondary metabolite transport. Here, the authors present the structure of the Arabidopsis thaliana MATE transporter AtDTX14 and propose a model for eukaryotic MATE transport mechanism. 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. 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. 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.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. Mulitidrug and toxic compound extrusion (MATE) family transporters export xenobiotics and some plant MATE transporters are involved in secondary metabolite transport. Here, the authors present the structure of the Arabidopsis thaliana MATE transporter AtDTX14 and propose a model for eukaryotic MATE transport mechanism. |
| ArticleNumber | 1633 |
| Author | Miyauchi, Hirotake Hirata, Kunio Kumazaki, Kaoru Nakane, Takanori Nureki, Osamu Nishizawa, Tomohiro Ishitani, Ryuichiro Moriyama, Satomi Yamashita, Keitaro Miyaji, Takaaki Moriyama, Yoshinori Dohmae, Naoshi Ito, Koichi Kusakizako, Tsukasa |
| Author_xml | – sequence: 1 givenname: Hirotake surname: Miyauchi fullname: Miyauchi, Hirotake organization: Department of Biological Sciences, Graduate School of Science, The University of Tokyo – sequence: 2 givenname: Satomi surname: Moriyama fullname: Moriyama, Satomi organization: Department of Membrane Biochemistry, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences – sequence: 3 givenname: Tsukasa surname: Kusakizako fullname: Kusakizako, Tsukasa organization: Department of Biological Sciences, Graduate School of Science, The University of Tokyo – sequence: 4 givenname: Kaoru surname: Kumazaki fullname: Kumazaki, Kaoru organization: Department of Biological Sciences, Graduate School of Science, The University of Tokyo – sequence: 5 givenname: Takanori orcidid: 0000-0003-2697-2767 surname: Nakane fullname: Nakane, Takanori organization: Department of Biological Sciences, Graduate School of Science, The University of Tokyo – sequence: 6 givenname: Keitaro orcidid: 0000-0002-5442-7582 surname: Yamashita fullname: Yamashita, Keitaro organization: RIKEN SPring-8 Center, Sayo-gun – sequence: 7 givenname: Kunio surname: Hirata fullname: Hirata, Kunio organization: RIKEN SPring-8 Center, Sayo-gun – sequence: 8 givenname: Naoshi surname: Dohmae fullname: Dohmae, Naoshi organization: Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Wako – sequence: 9 givenname: Tomohiro surname: Nishizawa fullname: Nishizawa, Tomohiro organization: Department of Biological Sciences, Graduate School of Science, The University of Tokyo – sequence: 10 givenname: Koichi surname: Ito fullname: Ito, Koichi organization: Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, The University of Tokyo – sequence: 11 givenname: Takaaki orcidid: 0000-0002-7257-7621 surname: Miyaji fullname: Miyaji, Takaaki organization: Advanced Science Research Center, Okayama University – sequence: 12 givenname: Yoshinori surname: Moriyama fullname: Moriyama, Yoshinori organization: Department of Membrane Biochemistry, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences – sequence: 13 givenname: Ryuichiro surname: Ishitani fullname: Ishitani, Ryuichiro email: ishitani@bs.s.u-tokyo.ac.jp organization: Department of Biological Sciences, Graduate School of Science, The University of Tokyo – sequence: 14 givenname: Osamu surname: Nureki fullname: Nureki, Osamu email: nureki@bs.s.u-tokyo.ac.jp organization: Department of Biological Sciences, Graduate School of Science, The University of Tokyo |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/29158478$$D View this record in MEDLINE/PubMed |
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| Snippet | Mulitidrug and toxic compound extrusion (MATE) family transporters export xenobiotics to maintain cellular homeostasis. The human MATE transporters mediate the... Mulitidrug and toxic compound extrusion (MATE) family transporters export xenobiotics and some plant MATE transporters are involved in secondary metabolite... |
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| Title | Structural basis for xenobiotic extrusion by eukaryotic MATE transporter |
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