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Excessive consumption of fructose in the Western diet is associated with an increased incidence of metabolic disorders such as obesity and non-alcoholic steatohepatitis. A growing interest is focused on the fructose transporter GLUT5. In this review, we describe crystal structures of the mammalian GLUT5 with its empty binding site exposed to either the extracellular side or intracellular side. By comparing structures in these two different conformational states, we show that the transport is achieved by a combination of global "rocker-switch"-like movement of transmembrane bundles and local asymmetric "gated-pore"-like rearrangement. This structural information is now open for designing novel therapeutic drugs

Structure and Molecular Mechanism of the Mammalian Fructose Transporter GLUT5