Review Article
Current Progress in the Structural and Biochemical Characterization of Proteins Involved in the Assembly of Lipopolysaccharide
Figure 11
WaaA. (a) WaaA bound to the CMP product (PDB: 2XCU) [78]. Spectrum coloring ends with red at the C-terminus. (b) Coulombic surface of WaaA from (a). Charge is shown with a blue-red scale with blue at the positive end. Bound polyethylene glycol molecules are shown. (c) Hydrophobicity surface of WaaA from (a). Hydrophobicity is shown on an orange-blue scale with orange as the hydrophobic end. The putative lipid IVA-binding pocket is circled. (d) Residues involved in CMP binding from (a). Hydrogen-bond and salt-bridge interactions are shown with the following distances in Ångstroms: 3.0 from phosphate to N273 N and 2.6 and 3.2 to R212 Nη1/2, 2.5 from E276 Oε1 to ribose 3′-hydroxyl and 2.8 to the 2′-hydroxyl, 2.9 from cytosine O2 to G248 N, and 3.1 from cytosine N4 to P211 O.
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