A division of labor for glycosylation

Glycobiology Glycosylation is a ubiquitous modification of eukaryotic secreted proteins. Asparagine-linked chains of sugars are appended to many substrates as they are translocated into the endoplasmic reticulum. Ramirez et al. solved cryo–electron microscopy structures of two human oligosaccharyltransferase complexes, OST-A and OST-B. The catalytic subunits bind partner proteins that direct glycosylation of specific substrates either cotranslationally (OST-A) or on fully folded proteins (OST-B). High-resolution views of the active site and bound substrates in one of the complexes reveal important features of the human enzymes. Science , this issue p. [1372][1] [1]: /lookup/doi/10.1126/science.aaz3505