Functional architecture of MFS D-glucose transporters

M. Gregor Madej, Linfeng Sun, Nieng Yan, H. Ronald Kaback

Research output: Contribution to journalArticlepeer-review

87 Scopus citations


The Major Facilitator Superfamily (MFS) is a diverse group of secondary transporters with over 10,000 members, found in all kingdoms of life, including Homo sapiens. One objective of determining crystallographic models of the bacterial representatives is identification and physical localization of residues important for catalysis in transporters with medical relevance. The recently solved crystallographic models of the D-xylose permease XylE from Escherichia coli and GlcP from Staphylococcus epidermidus, homologs of the human D-glucose transporters, the GLUTs (SLC2), provide information about the structure of these transporters. The goal of this work is to examine general concepts derived from the bacterial XylE, GlcP, and other MFS transporters for their relevance to the GLUTs by comparing conservation of functionally critical residues. An energy landscape for symport and uniport is presented. Furthermore, the substrate selectivity of XylE is compared with GLUT1 and GLUT5, as well as a XylE mutant that transports D-glucose.

Original languageEnglish (US)
Pages (from-to)E719-E727
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number7
StatePublished - Feb 18 2014

All Science Journal Classification (ASJC) codes

  • General


  • Glucose transport
  • Ligand docking
  • Membrane proteins
  • Sequence analysis
  • Solute carrier transporter


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