  2.4.1.B64 | an exposed and largely alpha-helical 30-residue sequence, with a net positive charge and several aromatic amino acids, is the putative membrane-interacting region of WaaG. In the presence of dodecylphosphocholine, the membrane-interacting region adopts a three-dimensional structure remarkably similar to the segment in the crystal structure. The interaction of WaaG is conferred at least in part by the membrane-interacting region and electrostatic interactions play a key role in binding. During anchoring of WaaG to the inner membrane of Escherichia coli, the central part of membrane-interacting region inserts into one leaflet of the bilayer. In this model, electrostatic interactions as well as surface-exposed Tyr residues bind WaaG to the membrane |
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