期刊
RESEARCH IN MICROBIOLOGY
卷 169, 期 7-8, 页码 384-392出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.resmic.2017.12.001
关键词
Antibiotic resistance; RND efflux pumps; AcrAB-TolC; Molecular dynamics; Molecular docking; Free energy calculations
类别
资金
- Innovative Medicines Initiative Joint Undertaking [115525]
- European Union's Seventh Framework Programme (FP7/2007-2013)
- EFPIA companies
- Marie Sklodowska-Curie fellow within the Translocation Network [607694]
The putative mechanism by which bacterial RND-type multidrug efflux pumps recognize and transport their substrates is a complex and fascinating enigma of structural biology. How a single protein can recognize a huge number of unrelated compounds and transport them through one or just a few mechanisms is an amazing feature not yet completely unveiled. The appearance of cooperativity further complicates the understanding of structure-dynamics-activity relationships in these complex machineries. Experimental techniques may have limited access to the molecular determinants and to the energetics of key processes regulating the activity of these pumps. Computer simulations are a complementary approach that can help unveil these features and inspire new experiments. Here we review recent computational studies that addressed the various molecular processes regulating the activity of RND efflux pumps. (C) 2018 The Authors. Published by Elsevier Masson SAS on behalf of Institut Pasteur.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据