Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 110, Issue 44, Pages 17862-17867Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1311485110
Keywords
major facilitator superfamily; membrane protein; GLUT; sugar transporter; solute-carrier 2A
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Funding
- National Institutes of Health [1R01DK091754]
- American Cancer Society [ILLBASIC00050068]
- United Nations Educational, Scientific and Cultural Organization-L'OREAL International Fellowships
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Glucose transporters are required to bring glucose into cells, where it is an essential energy source and precursor in protein and lipid synthesis. These transporters are involved in important common diseases such as cancer and diabetes. Here, we report the crystal structure of the Staphylococcus epidermidis glucose/H+ symporter in an inward-facing conformation at 3.2-angstrom resolution. The Staphylococcus epidermidis glucose/H+ symporter is homologous to human glucose transporters, is very specific and has high avidity for glucose, and is inhibited by the human glucose transport inhibitors cytochalasin B, phloretin, and forskolin. On the basis of the crystal structure in conjunction with mutagenesis and functional studies, we propose a mechanism for glucose/H+ symport and discuss the symport mechanism versus facilitated diffusion.
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