Structures of the acyl-substrate recognition motif.

<p>A) Alignment of the crystal structures of LasI (1R05 in blue) <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0112464#pone.0112464-Watson1" target="_blank">[18]</a> and EsaI (1KZF in red) <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0112464#pone.0112464-Gould1" target="_blank">[19]</a>. The two structures have a root-mean-square deviation of 1.45 Å for 124 amino acid α carbons. The conserved α-helix proposed to interact with ACP is circled in yellow. The active site cleft is behind this helix next to the conserved β-sheet. B) The LasI structure rotated 90° about the Z axis with positively-charged residues in the motif displayed.