EC Number   |
|---|
    6.3.1.20 | alone and in complex with lipoic acid |
| 6.3.1.20 | as apo form, in complex with ATP, and as lipoyl-AMP-complex. Lipoyl-AMP is bound deeply in the bifurcated pocket and adopts a U-shaped conformation |
| 6.3.1.20 | purified recombinant lipoyl-PfLipL1D243-279 complex, mixing of 0.001 ml of 5 mg/ml protein, 1.2 mol equiv of lipoate, and excess ATP with 0.001 ml of reservoir solution containing 100 mM HEPES, pH 7.0, 1.5 M (NH4)2SO4, and 20% ethylene glycol, 20°C, method optimization, X-ray diffraction structure determination and analysis at 2.32 A resolution |
| 6.3.1.20 | structural comparison of lipoate-protein ligase with cysteine/lysine dyad acyltransferase LipB shows conserved structural and sequence active-site features, but 4-phosphopantheine-bound octanoic acid recognition is a specific property of cysteine/lysine dyad acyltransferase |
| 6.3.1.20 | structural models of LplA1 and LplA2 based on Escherichia coli (PDB: 1X2H) and Streptococcus pneumoniae (PDB: 1VQZ) LplA proteins, conserved lipoyl-AMP binding pocket, LplA1: regions of clustered negatively charged residues, overall electrostatic potential of -13, LplA2: overall electrostatic potential of -5 |
