@article{168276,
  keywords = {Models, Molecular, Protein Conformation, Base Sequence, Humans, Biological Transport, Molecular Sequence Data, Binding Sites, Substrate Specificity, Sequence Analysis, DNA, Escherichia coli Proteins, Sequence Alignment, Escherichia coli O157, Sequence Homology, DNA, Complementary, Symporters, Glucose Transport Proteins, Facilitative, Calorimetry, Liposomes},
  author = {Gregor Madej and Linfeng Sun and Nieng Yan and Ronald Kaback},
  title = {Functional architecture of MFS D-glucose transporters},
  abstract = {<p>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.</p>
},
  year = {2014},
  journal = {Proc Natl Acad Sci U S A},
  volume = {111},
  pages = {E719-27},
  month = {02/2014},
  issn = {1091-6490},
  doi = {10.1073/pnas.1400336111},
  language = {eng},
}