Principles of Alternating Access in Multidrug and Toxin Extrusion (MATE) Transporters

被引：20

作者：

Claxton, Derek P. ^{[1
]}

Jagessar, Kevin L. ^{[1
]}

Mchaourab, Hassane S. ^{[1
]}

机构：

[1] Vanderbilt Univ, Dept Mol Physiol & Biophys, 747 Light Hall,2215 Garland Ave, Nashville, TN 37232 USA

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2021年 / 433卷 / 16期

关键词：

CONFORMATIONAL DYNAMICS; MOLECULAR-MECHANISMS; CRYSTAL-STRUCTURE; EFFLUX PUMPS; ION-BINDING; HYDROGEN/DEUTERIUM EXCHANGE; VIBRIO-PARAHAEMOLYTICUS; STAPHYLOCOCCUS-AUREUS; NEISSERIA-GONORRHOEAE; PROTEIN NORM;

D O I：

10.1016/j.jmb.2021.166959

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The multidrug and toxin extrusion (MATE) transporters catalyze active efflux of a broad range of chemically- and structurally-diverse compounds including antimicrobials and chemotherapeutics, thus contributing to multidrug resistance in pathogenic bacteria and cancers. Multiple methodological approaches have been taken to investigate the structural basis of energy transduction and substrate translocation in MATE transporters. Crystal structures representing members from all three MATE subfamilies have been interpreted within the context of an alternating access mechanism that postulates occupation of distinct structural intermediates in a conformational cycle powered by electrochemical ion gradients. Here we review the structural biology of MATE transporters, integrating the crystallographic models with biophysical and computational studies to define the molecular determinants that shape the transport energy landscape. This holistic analysis highlights both shared and disparate structural and functional features within the MATE family, which underpin an emerging theme of mechanistic diversity within the framework of a conserved structural scaffold. (C) 2021 Elsevier Ltd. All rights reserved.

引用

页数：19

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