title: Structural Biology of the Major Facilitator Superfamily Transporters.
abstract: The ancient and ubiquitous major facilitator superfamily (MFS) represents the largest secondary transporter family and plays a crucial role in a multitude of physiological processes. MFS proteins transport a broad spectrum of ions and solutes across membranes via facilitated diffusion, symport, or antiport. In recent years, remarkable advances in understanding the structural biology of the MFS transporters have been made. This article reviews the history, classification, and general features of the MFS proteins; summarizes recent structural progress with a focus on the sugar porter family transporters exemplified by GLUT1; and discusses the molecular mechanisms of substrate binding, alternating access, and cotransport coupling.
authors.affiliation: State Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Medicine, Tsinghua-Peking Joint Center for Life Sciences, Tsinghua University, Beijing 100084, China; email: nyan@tsinghua.edu.cn.
authors.forename: Nieng
authors.initials: N
authors.lastname: Yan
mesh_terms: D000818:Animals; D001419:Bacteria / Q000737:chemistry; D018360:Crystallography, X-Ray; D049673:History, 20th Century; D049674:History, 21st Century; D006801:Humans; D026901:Membrane Transport Proteins / Q000737:chemistry* / Q000235:genetics / Q000266:history / Q000378:metabolism
chemical_list: D026901:Membrane Transport Proteins
keywords: GLUT1; MFS; alternating access; major facilitator superfamily; membrane transport