 In mammals, glucose transporters, gluts, control organism-wide blood, glucose homeostasis. Human gluts are composed of 14 different isoforms, each of which transports glucose and other monosaccharides with varying substrate preferences and kinetics. Despite these differences, there is little difference between the sugar-coordinating residues in the glut proteins and even the malarial plasmodium falciparum transporter PFHT1, which is uniquely able to transport a wide range of different sugars. PFHT1 was captured in an intermediate, occluded, state, revealing how the extracellular gating helix TM7B had moved to break and occlude the sugar-binding site. Sequence difference and kinetics indicated that the TM7B gating helix dynamics and interactions likely evolved to enable substrate promiscuity in PFHT1, rather than the sugar-binding site itself. It was unclear, however, if the TM7B structural transitions observed in PFHT1 would be similar in the other glut proteins, using enhanced sampling molecular dynamics. This article was offered by Sarah E. McComis, Tom Reichenbach, Darko Mitrovich, and others. We are article.tv, links in the description below.