Abstract 1279 Structures of a mimiviral collagen glucosyltransferase reveal dimer assembly, substrate binding and cooperativity

Collagen glucosyltransferases catalyze a unique type of collagen glucosylation essential for biology and diseases. Yet, how collagen glucosyltransferases are structurally regulated is still not clear. Here we report the crystal structures of the collagen glucosyltransferase from Acanthamoeba polyphaga mimivirus with and without uridine diphosphate (UDP) and disaccharide product. The mimiviral glucosyltransferase is a homodimer stabilizing by a loop locking into a cleft in the opposite subunit. The dimer binds UDP glucose cooperatively, similar to a human homolog.