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

Figure 12

LpxM. (a) Ribbon diagram of LpxM (PDB: 5KN7) [86]. Spectrum coloring ends with red at the C-terminus. Interactions between putative catalytic residues are shown. Distances in Ångstroms are 2.6 from H122 Nδ to D192 Oδ1, 2.4 from E127 Oε1 to R159 Nη2 and 3.4 to Nη1, and 3.2 from E127 Oε2 to R159 Nη2. (b) Ligplot+ diagram of fatty acid binding to LpxM (PDB: 5KNK) with distance shown in Ångstroms [45, 86]. Hydrophobicity surface of LpxM (PDB: 5KNK). Hydrophobicity is shown on an orange-blue scale with blue as the hydrophilic end. The entrances to putative hydrocarbon-ruler channels are circled.

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