2.3.1.203	apo-crystal structures of the acetyltransferase domain ATD and in complex with AcCoA. The N-terminal section (Asn199-Leu285) comprises a binding pocket for the UDP-4-amino sugar substrate through a beta-alpha-beta-alpha-beta Rossman fold motif. The C-terminus (Pro286-Leu403) is composed of a left-handed beta-helix motif that, in conjunction with an adjacent PglB-ATD protomer in the trimeric state, forms an extended cleft that is utilized for AcCoA binding	
2.3.1.203	apoenzyme or in complex with CoA, hanging drop vapor diffusion method, using 0.1 M sodium acetate (pH 4.5) and 1.9 M ammonium sulfate, at 30°C	
2.3.1.203	compared to isoforms PglD and PglB, WeeI contains an additional loop (Gln174-Pro180) that forms the substrate binding pocket near the pyranose moiety. Residue Gln174 seems to be critical for catalysis. When aligned to the PglD UDP-4-amino structure, this position is analogous to Asn162 that interacts with the carbonyl oxygen of the pyranose C2-acetyl group. In the WeeI apo-structure, Gln174 is within 5 A of the catalytic base His138 and 3.6 A of the AcCoA thioester