title: Understanding transport by the major facilitator superfamily (MFS): structures pave the way.
abstract: Members of the major facilitator superfamily (MFS) of transport proteins are essential for the movement of a wide range of substrates across biomembranes. As this transport requires a series of conformational changes, structures of MFS transporters captured in different conformational states are needed to decipher the transport mechanism. Recently, a large number of MFS transporter structures have been determined, which has provided us with an unprecedented opportunity to understand general aspects of the transport mechanism. We propose an updated model for the conformational cycle of MFS transporters, the 'clamp-and-switch model', and discuss the role of so-called 'gating residues' and the substrate in modulating these conformational changes.
authors.affiliation: Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Scheeles väg 2, SE-17177 Stockholm, Sweden, the MIND Centre, Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 10C, DK 8000 Aarhus C, Denmark, and the Center for Structural Systems Biology (CSSB), European Molecular Biology Laboratory, EMBL-Hamburg, c/o DESY, Building 25A, Notkestrasse 85, 22607, Hamburg, Germany.
authors.forename: Esben M
authors.initials: EM
authors.lastname: Quistgaard
authors.affiliation: Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Scheeles väg 2, SE-17177 Stockholm, Sweden, and the Center for Structural Systems Biology (CSSB), European Molecular Biology Laboratory, EMBL-Hamburg, c/o DESY, Building 25A, Notkestrasse 85, 22607, Hamburg, Germany.
authors.forename: Christian
authors.initials: C
authors.lastname: Löw
authors.affiliation: Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Scheeles väg 2, SE-17177 Stockholm, Sweden.
authors.forename: Fatma
authors.initials: F
authors.lastname: Guettou
authors.affiliation: Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Scheeles väg 2, SE-17177 Stockholm, Sweden, and the School of Biological Sciences, Nanyang Technological University, 639798 Singapore, Singapore.
authors.forename: Pär
authors.initials: P
authors.lastname: Nordlund
mesh_terms: D000494:Allosteric Regulation; D000818:Animals; D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism; D001327:Autoimmune Diseases / Q000235:genetics / Q000378:metabolism* / Q000473:pathology; D001419:Bacteria / Q000235:genetics / Q000378:metabolism; D001692:Biological Transport; D002318:Cardiovascular Diseases / Q000235:genetics / Q000378:metabolism* / Q000473:pathology; D018360:Crystallography, X-Ray; D015870:Gene Expression; D006801:Humans; D026901:Membrane Transport Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure; D008958:Models, Molecular; D009369:Neoplasms / Q000235:genetics / Q000378:metabolism* / Q000473:pathology; D019636:Neurodegenerative Diseases / Q000235:genetics / Q000378:metabolism* / Q000473:pathology; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D026901:Membrane Transport Proteins