N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.
Comment:Active GlmU is trimeric, with active sites located at the interface between two LbH subunits. The trimer structure contains three active sites and each subunit contributes to two active sites via residues located on two surfaces.
Comment:The structure evidences show only the interaction of CoA and substrate to one interacting LbH subunit/surface.
Structure:2OI7_A; Escherichia coli GlmU binds Desulpho-CoA and GlcNAc-1-PO4; defined at 3.5A contacts. - View structure with Cn3D
Structure:2OI6_A; Escherichia coli GlmU binds CoA and GlcN-1-PO4; defined at 3.5A contacts. - View structure with Cn3D