Recent paradigm shift in the assembly of bacterial tripartite efflux pumps and the type I secretion system

被引：2

作者：

Jo, Inseong ^{[1
]}

Kim, Jin-Sik ^{[2
]}

Xu, Yongbin ^{[3
]}

Hyun, Jaekyung ^{[4
]}

Lee, Kangseok ^{[5
]}

Ha, Nam-Chul ^{[1
]}

机构：

[1] Seoul Natl Univ, Dept Agr Biotechnol, Ctr Food Safety & Toxicol, Ctr Food & Bioconvergence,Res Inst Agr & Life Sci, Seoul 08826, South Korea

[2] NICHHD, Unit Struct & Chem Biol Membrane Prot, Cell Biol & Neurobiol Branch, NIH, Bethesda, MD 20892 USA

[3] Dalian Minzu Univ, Dept Bioengn, Coll Life Sci, Dalian 116600, Liaoning, Peoples R China

[4] Korea Basic Sci Inst, Electron Microscopy Res Ctr, Cheongju 28119, South Korea

[5] Chung Ang Univ, Dept Life Sci, Seoul 06974, South Korea

来源：

JOURNAL OF MICROBIOLOGY | 2019年 / 57卷 / 03期

基金：

新加坡国家研究基金会;

关键词：

multidrug resistance; multidrug efflux pump; structure; cryo-electron microscopy; MEMBRANE-FUSION PROTEIN; RAY CRYSTALLOGRAPHIC ANALYSIS; MULTIDRUG TRANSPORTER ACRB; ALPHA-BARREL TIP; CRYSTAL-STRUCTURE; MACAB-TOLC; MACROLIDE TRANSPORTER; PERIPLASMIC COMPONENT; BINDING; REGION;

D O I：

10.1007/s12275-019-8520-1

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Tripartite efflux pumps and the type I secretion system of Gram-negative bacteria are large protein complexes that span the entire cell envelope. These complexes expel antibiotics and other toxic substances or transport protein toxins from bacterial cells. Elucidating the binary and ternary complex structures at an atomic resolution are crucial to understanding the assembly and working mechanism. Recent advances in cryoelectron microscopy along with the construction of chimeric proteins drastically shifted the assembly models. In this review, we describe the current assembly models from a historical perspective and emphasize the common assembly mechanism for the assembly of diverse tripartite pumps and type I secretion systems.

引用

页码：185 / 194

页数：10

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