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Literature DB >> 29193407

Thermodynamic secrets of multidrug resistance: A new take on transport mechanisms of secondary active antiporters.

Xuejun C Zhang^1,2, Min Liu^1,2, Guangyuan Lu^1,2, Jie Heng¹.

Abstract

Multidrug resistance (MDR) presents a growing challenge to global public health. Drug extrusion transporters play a critical part in MDR; thus, their mechanisms of substrate recognition are being studied in great detail. In this work, we review common structural features of key transporters involved in MDR. Based on our membrane potential-driving hypothesis, we propose a general energy-coupling mechanism for secondary-active antiporters. This putative mechanism provides a common framework for understanding poly-specificity of most-if not all-MDR transporters.

Keywords: energy coupling; exporters; membrane potential; multidrug resistance; titratable residue

Mesh：

Substances：

Year: 2017 PMID： 29193407 PMCID： PMC5818768 DOI： 10.1002/pro.3355

Source DB: PubMed Journal: Protein Sci ISSN： 0961-8368 Impact factor: 6.725

78 in total

1. Structure and mechanism of the lactose permease of Escherichia coli.

Authors: Jeff Abramson; Irina Smirnova; Vladimir Kasho; Gillian Verner; H Ronald Kaback; So Iwata
Journal: Science Date: 2003-08-01 Impact factor: 47.728

2. Mechanical coupling of the multiple structural elements of the large-conductance mechanosensitive channel during expansion.

Authors: Jie Li; Jianli Guo; Xiaomin Ou; Mingfeng Zhang; Yuezhou Li; Zhenfeng Liu
Journal: Proc Natl Acad Sci U S A Date: 2015-08-10 Impact factor: 11.205

Review 3. Ins and outs of major facilitator superfamily antiporters.

Authors: Christopher J Law; Peter C Maloney; Da-Neng Wang
Journal: Annu Rev Microbiol Date: 2008 Impact factor: 15.500

4. Simple allosteric model for membrane pumps.

Authors: O Jardetzky
Journal: Nature Date: 1966-08-27 Impact factor: 49.962

5. The First Nucleotide Binding Domain of Cystic Fibrosis Transmembrane Conductance Regulator Is a Site of Stable Nucleotide Interaction, whereas the Second Is a Site of Rapid Turnover.

Authors: Luba Aleksandrov; Andrei A Aleksandrov; Xiu-Bao Chang; John R Riordan
Journal: J Biol Chem Date: 2002-02-22 Impact factor: 5.157

Thermodynamic secrets of multidrug resistance: A new take on transport mechanisms of secondary active antiporters.

1. Structure and mechanism of the lactose permease of Escherichia coli.

2. Mechanical coupling of the multiple structural elements of the large-conductance mechanosensitive channel during expansion.

Review 3. Ins and outs of major facilitator superfamily antiporters.

4. Simple allosteric model for membrane pumps.

5. The First Nucleotide Binding Domain of Cystic Fibrosis Transmembrane Conductance Regulator Is a Site of Stable Nucleotide Interaction, whereas the Second Is a Site of Rapid Turnover.

6. Structural basis of MsbA-mediated lipopolysaccharide transport.

7. Crystal structures of the PsbS protein essential for photoprotection in plants.

8. Uniporter substrate binding and transport: reformulating mechanistic questions.

9. Energy coupling mechanisms of AcrB-like RND transporters.

10. Structural insights into H+-coupled multidrug extrusion by a MATE transporter.

Review 1. Interplay between the electrostatic membrane potential and conformational changes in membrane proteins.

2. smFRET Probing Reveals Substrate-Dependent Conformational Dynamics of E. coli Multidrug MdfA.

3. Dissection of Protonation Sites for Antibacterial Recognition and Transport in QacA, a Multi-Drug Efflux Transporter.

4. Asymmetric protonation of glutamate residues drives a preferred transport pathway in EmrE.

5. TrkA undergoes a tetramer-to-dimer conversion to open TrkH which enables changes in membrane potential.