EC Number   |
|---|
    2.3.1.191 | apo forms of LpxD in space groups P21 and P4322, to 2.7 and 2.8 A resolution, respectively. The asymmetric unit contains two protein trimers |
| 2.3.1.191 | enzyme in complex with 4-(2-chlorophenyl)-3-hydroxy-7,7-dimethyl-2-phenyl-7,8-dihydro-2H-pyrazolo[3,4-b]quinolin-5(6H)-one. Enzyme in complex with 3-hydroxy-7,7-dimethyl-2-phenyl-4-(thiophen-2-yl)-7,8-dihydro-2H-pyrazolo[3,4-b]-quinolin-5(6H)-one |
| 2.3.1.191 | hanging drop vapor diffusion. Crystallographic analyses of recombinant Chlamydia trachomatis LpxD in complex with UDP-GlcNAc, which represents a fragment of substrate, and fatty acid extracted from the bacterial expression system, apo-structure at 2.7 A resolution, and two structures with bound UDP-N-acetylglucosamine (UDP-GlcNAc) at 2.2 A and 3.1 A resolution |
| 2.3.1.191 | hanging drop/vapor diffusion method. The crystal structure of N-terminally His6-tagged EcLpxD is determined by molecular replacement at 2.6 A resolution, using Chlamydia trachomatis (PDB code: 2IUA) as the model. Comparison of LpxD from Escherichia coli and Chlamydia trachomatis. Attempts to crystallize EcLpxD with UDP-GlcNAc, UDP-3-O-(R-3-hydroxymyristoyl)-R-D-GlcNAc or its product UDP-2,3-diacylglucosamine are unsuccessful |
| 2.3.1.191 | in complex with three forms of acyl carrier protein. Interactions at the interface optimally position acyl carrier protein for acyl delivery and directly involve the pantetheinyl group |
| 2.3.1.191 | purified recombinant His6-tagged LpxD, hanging drop vapour diffusion, 0.002 ml of 15 mg/ml LpxD in 10 mM Tris pH 8, 500 mM NaCl and 1 mM DTT, with 50 mM uridine diphosphate-N-acetylglucosamine, is mixed with 0.002 ml of 100 mM Tris pH 8.5, 1.5 M lithium sulfate, 20°C, 3-5 days, X-ray diffraction structure determination and analysis at 1.3 A resolution, molecular replacement |
