Structure and mechanism of the bacterial lipid ABC transporter,MlaFEDB |
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| Institution: | 1. Department of Cell Biology, New York University School of Medicine, New York, NY, USA;2. Department of Microbiology, New York University School of Medicine, New York, NY, USA;1. School of Physics and Optoelectronic Engineering, Xidian University, Xi’an 710126, China;2. China Research Institute of Radiowave Propagation (CRIRP), Qingdao 266107, China;1. Institute of Biochemistry, Heinrich-Heine-Universität Düsseldorf, Universitätsstraße 1, 40225 Düsseldorf, Germany;2. Department of Life Sciences and Chemistry, Jacobs University Bremen, 28719 Bremen, Germany;3. Center for Structural Studies Heinrich-Heine-Universität Düsseldorf, Universitätsstraße 1, 40225 Düsseldorf, Germany;4. Institute of Pharmaceutical and Medicinal Chemistry, Heinrich-Heine-Universität Düsseldorf, Universitätsstraße 1, 40225 Düsseldorf, Germany;5. Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW, United Kingdom;6. Institute for Medical Physics and Biophysics and Center for Soft Nanoscience, Westfälische Wilhelms Universität Münster, 48149 Münster, Germany;7. Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany;1. Molecular Microbiology & Structural Biochemistry (MMSB) UMR 5086, CNRS/University of Lyon, Lyon 69367, France;2. IBS, Univ. Grenoble Alpes, CNRS, CEA, Grenoble 38000, France;3. Institut Max Von Laue Paul Langevin (ILL), Grenoble 38000, France;4. Institut de Pharmacologie et de Biologie Structurale, Université de Toulouse, CNRS, Toulouse, 31000, France;1. Ministry of Education Key Laboratory of Protein Sciences, Tsinghua University, Beijing, China;2. Beijing Advanced Innovation Center for Structural Biology, Tsinghua University, Beijing, China;3. School of Life Sciences, Tsinghua University, Beijing, China;4. Tsinghua-Peking Joint Center for Life Sciences, Beijing, China |
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| Abstract: | The cell envelope of Gram-negative bacteria is composed of an inner membrane, outer membane, and an intervening periplasmic space. How the outer membrane lipids are trafficked and assembled there, and how the asymmetry of the outer membrane is maintained is an area of intense research. The Mla system has been implicated in the maintenance of lipid asymmetry in the outer membrane, and is generally thought to drive the removal of mislocalized phospholipids from the outer membrane and their retrograde transport to the inner membrane. At the heart of the Mla pathway is a structurally unique ABC transporter complex in the inner membrane, called MlaFEDB. Recently, an explosion of cryo-EM studies has begun to shed light on the structure and lipid translocation mechanism of MlaFEDB, with many parallels to other ABC transporter families, including human ABCA and ABCG, as well as bacterial lipopolysaccharide and O-antigen transporters. Here we synthesize information from all available structures, and propose a model for lipid trafficking across the cell envelope by MlaFEDB. |
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