Primate-specific regulation of the human glycosphingolipid gatekeeper UGCG

TL;DR - Cryogenic electron microscopy structures reveal how full-length human UGCG, a key regulator of glycosphingolipid diversity, catalyses its reaction. The findings identify a metal-independent mechanism driven by an arginine network.

• Reports cryo-EM structures of full-length human UGCG.
• UGCG controls the scale and composition of glycosphingolipid diversity.
• The structures indicate that catalysis does not require a metal cofactor.
• An arginine network drives the proposed catalytic mechanism.