<p>A, Schematic representation of the mutations introduced in the rescue constructs encoding dEndoA-BAR. B, Mutations homologous to the mutations in dEndoA-BAR (A), mapped onto the tertiary structure of hEndoA1-BAR monomer <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0009492#pone.0009492-Masuda1" target="_blank">[PDB code 1X03A, 8]</a>. The central helix-loop appendage (<i>red</i>) and the residues constituting the hydrophobic ridge (<i>yellow</i>) are indicated. The residues mutated to change the BAR domain curvature are also indicated (<i>pink</i>), as are the three electropositive lysine residues that were mutated to electronegative glutamic acid residues (<i>light green</i>). The <i>inset</i> at the lower right shows the BAR dimer, with the two monomers colored <i>gray</i> and <i>blue</i>. C, Primary structure alignment of hEndoA1-BAR (accession BAE44459.1; <i>top</i>) and dEndoA-BAR (accession CAD24682.1; <i>bottom</i>). The alpha-helical secondary structure is indicated by <i>squiggles</i>, based on the hEndoA1-BAR structure. The residues associated with the hydrophobic ridge are also indicated (<i>closed triangles</i>).</p
