Glycosyltransferases (GTs) catalyze the addition of sugars to diverse substrates. When embedded in or associated with the membrane, these enzymes often rely on polyisoprenyl-phosphate or -pyrophosphate (PP) lipid carriers to transfer glycan moieties. Here, Rie will present different bacterial GT structures and compare their substrate binding mechanisms. Additionally, she will present how they successfully visualized how the GtrB enzyme transitions during the catalytic cycle. Using time-resolved cryo-EM, multiple distinct conformational states: the initial substrate-bound state, a catalytically poised intermediate, and the product-bound state, were identified.
