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Tytuł:
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Structural biology of the multidrug and toxic compound extrusion superfamily transporters.
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Autorzy:
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Kusakizako T; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
Miyauchi H; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
Ishitani R; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan. Electronic address: .
Nureki O; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan. Electronic address: .
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Źródło:
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Biochimica et biophysica acta. Biomembranes [Biochim Biophys Acta Biomembr] 2020 Dec 01; Vol. 1862 (12), pp. 183154. Date of Electronic Publication: 2019 Dec 19.
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Typ publikacji:
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Journal Article; Research Support, Non-U.S. Gov't; Review
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Język:
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English
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Imprint Name(s):
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Original Publication: Amsterdam : Elsevier
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MeSH Terms:
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ATP-Binding Cassette Transporters/*metabolism
Organic Cation Transport Proteins/*metabolism
Plant Proteins/*metabolism
ATP-Binding Cassette Transporters/chemistry ; ATP-Binding Cassette Transporters/classification ; Archaea/metabolism ; Archaeal Proteins/chemistry ; Archaeal Proteins/classification ; Archaeal Proteins/metabolism ; Humans ; Molecular Dynamics Simulation ; Organic Cation Transport Proteins/chemistry ; Organic Cation Transport Proteins/classification ; Plant Proteins/chemistry ; Plant Proteins/classification ; Plants/metabolism ; Protein Structure, Tertiary ; Substrate Specificity
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Contributed Indexing:
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Keywords: Crystal structure; MATE superfamily; Multi-drug resistance; Structural biology; Transporter
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Substance Nomenclature:
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0 (ATP-Binding Cassette Transporters)
0 (Archaeal Proteins)
0 (Organic Cation Transport Proteins)
0 (Plant Proteins)
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Entry Date(s):
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Date Created: 20191224 Date Completed: 20201229 Latest Revision: 20201229
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Update Code:
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20240105
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DOI:
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10.1016/j.bbamem.2019.183154
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PMID:
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31866287
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Xenobiotic and metabolite extrusion is an important process for the proper functions of cells and their compartments, including acidic organelles. MATE (multidrug and toxic compound extrusion) is a large family of secondary active transporters involved in the transport of various compounds across cellular and organellar membranes, and is present in the three domains of life. The major substrates of the bacterial MATE transporters are cationic compounds, including clinically important antibiotics, and thereby MATE transporters confer multi-drug resistance to pathogenic bacteria. The plant MATE transporters are important for the accumulation of various metabolites in organelles, including vacuoles. The human MATE transporters are expressed in the brush-border membrane of the kidney, and are involved in the clearance of cationic drugs from the body. During the past decade, progress in structural biology has clarified the transport mechanism of these MATE transporters in atomic detail. The present review summarizes the reported structures of MATE family transporters, along with their structure-guided functional analyses. This integrated view of the structures of MATE transporters provides novel insights into their transport mechanism.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2019 The Author(s). Published by Elsevier B.V. All rights reserved.)
