Current Progress in the Structural and Biochemical Characterization of Proteins Involved in the Assembly of Lipopolysaccharide

Figure 8

LpxI. (a) LpxI dimer bound to lipid X (PDB: 4GGM) [55]. (b) LpxI-D225 A dimer bound to UDP-DAG (PDB: 4J6E) [55]. (c) Residues involved in UDP-DAG binding to LpxI-D225 A from (b). Hydrogen-bond and salt-bridge interactions are shown, and the distance between A225 and the β-phosphate is highlighted. Distances in Ångstroms are as follows: 3.3 from 3′-acyl carbonyl to L226 N 2.5 from ribose 2′-hydroxyl to D188 Oδ2, 2.3 from ribose 3′-hydroxyl to D188 Oδ1 and 3.0 to T233 Oγ, 3.3 from α-phosphate to T187 N and 2.8 to T187 Oγ and 3.3 to K214 Nζ, 2.6 from β-phosphate to K214 Nζ and 2.9 to Q169 Nε, 2.5 from glucosamine 4′-hydroxyl to T228 Oγ, 3.3 from uracil O2 to A232 N 2.9 from the glucosamine ring O to N74 Nδ, 3.4 from uracil O4 to A12 N, and 3.1 from 2′-acyl carbonyl to V75 N.

(a)

(b)

(c)