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序列偏差在多药转运蛋白EmrE拓扑结构中的作用。

Role of sequence bias in the topology of the multidrug transporter EmrE.

作者信息

McHaourab Hassane S, Mishra Sanjay, Koteiche Hanane A, Amadi Sepan H

机构信息

Department of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, Tennessee 37232-0615, USA.

出版信息

Biochemistry. 2008 Aug 5;47(31):7980-2. doi: 10.1021/bi800628d. Epub 2008 Jul 11.

DOI:10.1021/bi800628d
PMID:18616286
Abstract

EmrE is the prototype of small multidrug resistance transporters and has emerged as a model of membrane protein evolution. Analysis of the distances separating symmetry-related site-specific spin labels, correlation of topological sequence bias to C-terminal orientation, to membrane insertion efficiency, and to resistance to ethidium bromide collectively demonstrate that EmrE monomers adopt a parallel topology in the functional dimer. We propose a coupled insertion and assembly model for EmrE in which the favorable energetics of the parallel dimer interface override topological constraints arising from weak asymmetry in positive charge distribution.

摘要

EmrE是小多药耐药转运蛋白的原型,已成为膜蛋白进化的一个模型。对对称相关位点特异性自旋标记之间距离的分析、拓扑序列偏差与C端方向、膜插入效率以及对溴化乙锭抗性的相关性分析共同表明,EmrE单体在功能性二聚体中采用平行拓扑结构。我们提出了一种EmrE的耦合插入和组装模型,其中平行二聚体界面有利的能量克服了由正电荷分布的弱不对称性产生的拓扑限制。

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Role of sequence bias in the topology of the multidrug transporter EmrE.序列偏差在多药转运蛋白EmrE拓扑结构中的作用。
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2
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Undecided membrane proteins insert in random topologies. Up, down and sideways: it does not really matter.
未确定的膜蛋白以任意拓扑结构插入。向上、向下或侧向:实际上并不重要。
Trends Biochem Sci. 2012 Jun;37(6):215-9. doi: 10.1016/j.tibs.2012.02.006. Epub 2012 Mar 21.
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Antiparallel EmrE exports drugs by exchanging between asymmetric structures.反平行 EmrE 通过在不对称结构之间交换来输出药物。
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Analyzing conformational changes in the transport cycle of EmrE.分析 EmrE 转运循环中的构象变化。
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Structure, dynamics, and substrate-induced conformational changes of the multidrug transporter EmrE in liposomes.脂质体中多药转运蛋白 EmrE 的结构、动态特性和底物诱导的构象变化。
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