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. Author manuscript; available in PMC: 2018 Nov 1.
Published in final edited form as: Biochim Biophys Acta. 2016 Dec 9;1862(11):1424–1438. doi: 10.1016/j.bbalip.2016.11.014

Figure 2. Structure and inhibition of LpxA.

Figure 2

(A) Structure of the E. coli LpxA/UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc complex (PDB: 2qia). LpxA consists of a homotrimer, with each monomer labeled in distinct colors. The domains and termini of the green monomer are labeled. LpxA is shown in the ribbon diagram, whereas the UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc molecules are shown in the space-filling model. (B) The hydrocarbon rulers of LpxA enzymes from E. coli (PDB: 2qia), L. interrogans (PDB: 3i3x), and P. aeruginosa (PDB: 5dg3). (C) LpxA acyl chain selectivity and catalysis. (D) Overlay of UDP-3-N-(R-3-hydroxylauroyl)-GlcNAc3N (grey) and R-3-hydroxylauroylmethylphosphopantetheine (yellow) in the L. interrogans LpxA complexes (PDB: 3i3x and 3i3a). UDP-3-N-(R-3-hydroxylauroyl)-GlcNAc3N and R-3-hydroxylauroylmethyl-phosphopantetheine are shown in the stick model. The catalytic dyads are labeled, with Lepstopira residue numbers shown in black and E. coli residue numbers shown in red. (E) Peptide 920 bound to E. coli LpxA (PDB: 2aq9). (F) Peptide RJPXD33 bound to E. coli LpxA (PDB: 4j09). Carbon atoms of peptides in panels (E) and (F) are colored in yellow, whereas carbon atoms of UDP-3-O-acyl-GlcNAc are colored in grey.