@article{168151,
  keywords = {Models, Molecular, Protein Conformation, Crystallography, X-Ray, Humans, Biological Transport, Escherichia coli, Structure-Activity Relationship, Substrate Specificity, Escherichia coli Proteins, Glucose, Structural Homology, Protein, Hydrogen Bonding, Symporters, xylose, Glucose Transporter Type 1, Glucose Transport Proteins, Facilitative, Deoxyglucose},
  author = {Linfeng Sun and Xin Zeng and Chuangye Yan and Xiuyun Sun and Xinqi Gong and Yu Rao and Nieng Yan},
  title = {Crystal structure of a bacterial homologue of glucose transporters GLUT1-4},
  abstract = {<p>Glucose transporters are essential for metabolism of glucose in cells of diverse organisms from microbes to humans, exemplified by the disease-related human proteins GLUT1, 2, 3 and 4. Despite rigorous efforts, the structural information for GLUT1-4 or their homologues remains largely unknown. Here we report three related crystal structures of XylE, an Escherichia coli homologue of GLUT1-4, in complex with d-xylose, d-glucose and 6-bromo-6-deoxy-D-glucose, at resolutions of 2.8, 2.9 and 2.6 {\r A}, respectively. The structure consists of a typical major facilitator superfamily fold of 12 transmembrane segments and a unique intracellular four-helix domain. XylE was captured in an outward-facing, partly occluded conformation. Most of the important amino acids responsible for recognition of D-xylose or d-glucose are invariant in GLUT1-4, suggesting functional and mechanistic conservations. Structure-based modelling of GLUT1-4 allows mapping and interpretation of disease-related mutations. The structural and biochemical information reported here constitutes an important framework for mechanistic understanding of glucose transporters and sugar porters in general.</p>
},
  year = {2012},
  journal = {Nature},
  volume = {490},
  pages = {361-6},
  month = {10/2012},
  issn = {1476-4687},
  doi = {10.1038/nature11524},
  language = {eng},
}