• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Nature >Antiparallel EmrE exports drugs by exchanging between asymmetric structures
【24h】

Antiparallel EmrE exports drugs by exchanging between asymmetric structures

机译：反平行EmrE通过不对称结构之间的交换来出口药物

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Small multidrug resistance transporters provide an ideal system to study the minimal requirements for active transport. EmrE is one such transporter in Escherichia coli. It exports a broad class of polyaromatic cation substrates, thus conferring resistance to drug compounds matching this chemical description. However, a great deal of controversy has surrounded the topology of the EmrE homodimer. Here we show that asymmetric antiparallel EmrE exchanges between inward- and outward-facing states that are identical except that they have opposite orientation in the membrane. We quantitatively measure the global conformational exchange between these two states for substrate-bound EmrE inbicelles using solution NMR dynamics experiments. Forster resonance energy transfer reveals that the monomers within each dimer are antiparallel, and paramagnetic relaxation enhancement NMR experiments demonstrate differential water accessibility of the two monomers within each dimer. Our experiments reveal a 'dynamic symmetry' that reconciles the asymmetric EmrE structure with the functional symmetry of residues in the active site.
机译：小型的多药耐药转运蛋白为研究主动转运的最低要求提供了理想的系统。 EmrE是大肠杆菌中的一种此类转运蛋白。它可以输出种类繁多的聚芳族阳离子底物，从而赋予对与该化学描述相匹配的药物化合物的抗性。但是，EmrE同型二聚体的拓扑结构存在许多争议。在这里，我们表明，向内和向外的状态之间的不对称反平行EmrE交换是相同的，只是它们在膜中具有相反的方向。我们使用溶液NMR动力学实验定量测量了这两种状态之间的整体构象交换，用于底物结合的EmrE本体。 Forster共振能量转移表明，每个二聚体中的单体是反平行的，顺磁弛豫增强NMR实验表明，每个二聚体中的两个单体的水可及性不同。我们的实验揭示了一种“动态对称性”，可将不对称的EmrE结构与活性位点中残基的功能对称性相协调。

著录项

  • 来源
    《Nature》 |2012年第7379期|p.45-50|共6页
  • 作者

    Emma A. Morrison; Gregory T. DeKoster; Supratik Dutta; Reza Vafabakhsh; Michael W. Clarkson; Arjun Bahl; Dorothee Kern; Taekjip Ha; Katherine A. Henzler-Wildman;

  • 作者单位

    Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110, USA.;

    Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110, USA.;

    Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110, USA.;

    Department of Physics and Howard Hughes Medical Institute,University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.;

    Department of Biochemistry and Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454, USA;

    Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110, USA.;

    Department of Biochemistry and Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454, USA;

    Department of Physics and Howard Hughes Medical Institute,University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.;

    Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110, USA;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号