EC Number   |
|---|
    2.3.1.129 | by the sitting-drop, vapour-diffusion method using 0.00l ml of protein solution |
| 2.3.1.129 | by using the hanging drop vapor diffusion method, in the presence of a 25-fold molar excess of either UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc or UDP-3-O-(R-3-hydroxydecanoyl)-GlcNAc, structures show how LpxA selects for 14-carbon R-3-hydroxyacyl chains and reveal two modes of UDP binding |
| 2.3.1.129 | crystal structures of free LiLpxA and its complexes with its product UDP-3-N-((R)-3-hydroxylauroyl)-GlcNAc3N and with its substrate (R)-3-hydroxylauroyl-methylphosphopantetheine are presented. The selectivity of LiLpxA for UDPGlcNAc3N may be explained by the orientation of the backbone carbonyl group of Q68, which differs by 82° from the corresponding Q73 carbonyl group in Escherichia coli LpxA. This arrangement provides an extra hydrogen-bond acceptor for the 3-NH2 group of UDP-GlcNAc3N in LiLpxA. The R-3-hydroxylauroyl selectivity of LiLpxA is explained by the position of the K171 side chain, which limits the length of the acyl-chain-binding groove. H120 functions as a catalytic base |
| 2.3.1.129 | crystallized at 297 K using (NH4)2SO4 and Na/K tartrate as precipitants in the presence of a detergent, space group: P6322 with unit cell-parameters: a = b = 90.69, and c = 148.20 ANG |
| 2.3.1.129 | in complex with inhibitor peptide WMLDPIAGKWSR, to 1.6 A resolution. The peptide is located at the interface of each adjacent subunit and interacts with residues from both sides. It occupies part of the ACP binding site |
| 2.3.1.129 | LpxA in complex with UDP-GlcNAc, modelling |
| 2.3.1.129 | purified enzyme LpxA in a complex with inhibitor peptide 920, 20 mg/ml protein in solution with a 25fold molar excess of peptide 920 of 12.5 mM, crystal growth at 18°C, hanging drop vapor diffusion method, mixing of 0.002 ml protein solution with 0.002 ml of 0.81.8 M phosphate buffer, pH 6.36.9, and 30-35% DMSO, about 2 weeks, X-ray diffraction structure determination and analysis at 1.8 A resolution, molecular replacement using crystal structure PDB ID code 1LXA, determined at 2.6 A resolution |
| 2.3.1.129 | purified recombinant LpxA, sitting drop vapor diffusion method, mixing of AtLpxA at 18 mg/mL in 10 mM potassium phosphate buffer, pH 7.0, 200 mM KCl, and 20% glycerol, in a 1:1 ratio with precipitant solution containing 0.5 M ammonium sulfate, 0.1 M sodium citrate, pH 5.6, and 1.0 M lithium sulfate monohydrate, equilibration at 20°C, 1-2 days, X-ray diffraction structure determination and analysis at 2.1 A resolution |
| 2.3.1.129 | purified recombinant, C-terminally eight-residue-tagged enzyme, X-ray diffraction structure analysis at 2.1 A resolution, modeling of the enzyme complexed with [acyl-carrier protein] |
| 2.3.1.129 | structure in complex with peptide RJPXD33 at 1.9 A resolution. Results suggest that the peptide binds in a unique modality that mimics (R)-beta-hydroxyacyl pantetheine binding to LpxA. REsidue H160 changes its conformation upon binding of peptide. Overlay of the LpxA RJPXD33 structure with LpxD, EC 2.31.191, identifies a complementary peptide binding pocket within LpxD and serves as a model for characterization of RJPXD33 binding to LpxD |
