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	736434	
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	718849	
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	736434