Assembly and operation of bacterial tripartite multidrug efflux pumps

被引：60

作者：

Du, Dijun ^{[1
]}

van Veen, Hendrik W. ^{[2
]}

Luisi, Ben F. ^{[1
]}

机构：

[1] Univ Cambridge, Dept Biochem, Cambridge CB2 1GA, England

[2] Univ Cambridge, Dept Pharmacol, Cambridge CB2 1PD, England

来源：

TRENDS IN MICROBIOLOGY | 2015年 / 23卷 / 05期

基金：

英国生物技术与生命科学研究理事会; 英国惠康基金; 英国医学研究理事会;

关键词：

membrane proteins; drug resistance; transport mechanism; MAJOR FACILITATOR SUPERFAMILY; PERIPLASMIC ADAPTER PROTEIN; OUTER-MEMBRANE PROTEIN; X-RAY-STRUCTURE; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; ATP-BINDING; TIP REGION; PSEUDOMONAS-AERUGINOSA; ALTERNATING ACCESS;

D O I：

10.1016/j.tim.2015.01.010

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：

Microorganisms encode several classes of transmembrane pumps that can expel an enormous range of toxic substances, thereby improving their fitness in harsh environments and contributing to resistance against antimicrobial agents. In Gram-negative bacteria these pumps can take the form of tripartite assemblies that actively efflux drugs and other harmful compounds across the cell envelope. We describe recent structural and functional data that have provided insights into the transport mechanisms of these intricate molecular machines.

引用

页码：311 / 319

页数：9

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