title: Structural basis for substrate transport in the GLUT-homology family of monosaccharide transporters.
abstract: Here we present two structures of the major facilitator (MFS) xylose transporter XylE from Escherichia coli in inward open and partially occluded inward open conformations. These structures provide key information about the transport cycle of XylE and the closely related human GLUT transporters. This is, to our knowledge, the first MFS transporter structure determined in more than one conformational state, which may establish XylE as an important MFS model protein.
authors.affiliation: Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
authors.forename: Esben M
authors.initials: EM
authors.lastname: Quistgaard
authors.forename: Christian
authors.initials: C
authors.lastname: Löw
authors.forename: Per
authors.initials: P
authors.lastname: Moberg
authors.forename: Lionel
authors.initials: L
authors.lastname: Trésaugues
authors.forename: Pär
authors.initials: P
authors.lastname: Nordlund
mesh_terms: D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry / Q000201:enzymology* / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D011487:Protein Conformation; D027981:Symporters / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D029968:Escherichia coli Proteins; D027981:Symporters; C033903:xylE protein, E coli